499:
467:. Following sIV, loop Gln186-Gly192 and β-strand sV are responsible for contributing with many ligands to the several metal ions present in the protein (read further). A large open loop follows sV which has proven importance in substrate specificity within the MMPs family. A specific region (183)RWTNNFREY(191) has been identified as a critical segment of matrix metalloproteinase 1 for the expression of collagenolytic activity. On C-terminal part of the CAT Domain the hB α-helix, known as the "active-site helix" encompasses part of the "zinc-binding consensus sequence" HEXXHXXGXXH that is characteristic of the
1720:
1750:
1660:
1690:
1735:
1705:
1600:
1585:
1615:
1570:
1675:
1630:
1645:
2466:
463:
bridging sII to sIII. Following the sIII strand the sequence meets the 'S-shaped double loop' that is of primary importance for the peptide structure and catalytic activity (see further) as it extends to the cleft side "bulge", continuing to the only antiparallel β-strand sIV, which is prime importance for binding peptidic substrates or inhibitors by forming main chain
458:
The catalytic domain (CAT) of MMP-1 starts with the F100 (non-truncated CAT) as the first amino-acid of the N-terminal loop of the CAT domain. The first published x-ray structure of the CAT domain was representative of the truncated form of this domain, where the first 7 amino-acids are not present.
462:
After the initial loop, the sequences follows to the first and longest β-sheet (sI). A second loop precedes large "amphipathic α-helix" (hA) that longitudinally spans protein site. The β-strands sII and sIII follows separated by the respective loops, loop 4 being commonly designated as "short loop"
441:
The catalytic domains of MMPs share very similar characteristics, having a general shape of oblate ellipsoid with a diameter of ~40 Ă…. Despite the similarity of the catalytic domains of MMPs, this entry will focus only on the structural features of MMP-1 catalytic domain.
1044:
Bode W, Gomis-Rüth FX, Stöckler W (September 1993). "Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'".
432:
Two main nomenclatures for the primary structure are currently in use, the original one from which the first amino-acid starts with the signalling peptide and a second one where the first amino-acid starts counting from the prodomain (proenzyme nomenclature).
471:. The α-helix hB finishes abruptly at Gly225 where the last loop of the domain starts. This last loop contains the "specificity loop" which is the shortest in the MMPs family. The Catalytic Domain ends at Gly261 with α-helix hC.
1137:
Huang SF, Li YH, Ren YJ, Cao ZG, Long X (August 2008). "The effect of a single nucleotide polymorphism in the matrix metalloproteinase-1 (MMP-1) promoter on force-induced MMP-1 expression in human periodontal ligament cells".
486:
in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Specifically, MMP-1 breaks down the interstitial
454:
of MMP-1 is composed of five highly twisted β-strands (sI-sV), three α-helix (hA-hC) and a total of eight loops, enclosing a total of five metal ions, three Ca and two Zn, one of which with catalytic role.
1719:
535:
Mechanical force may increase the expression of MMP1 in human periodontal ligament cells. During cancer progression, MMP1 can be dysregulated by different mechanisms, including the activation of an
1749:
917:
Spurlino JC, Smallwood AM, Carlton DD, Banks TM, Vavra KJ, Johnson JS, Cook ER, Falvo J, Wahl RC, Pulvino TA (June 1994). "1.56 A structure of mature truncated human fibroblast collagenase".
1659:
498:
1689:
1734:
1704:
670:
Pendás AM, SantamarĂa I, Alvarez MV, Pritchard M, LĂłpez-OtĂn C (October 1996). "Fine physical mapping of the human matrix metalloproteinase genes clustered on chromosome 11q22.3".
1599:
1584:
1614:
1569:
1674:
1090:"The metzincins--topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases"
1790:
1629:
1644:
1005:"Identification of the (183)RWTNNFREY(191) region as a critical segment of matrix metalloproteinase 1 for the expression of collagenolytic activity"
1267:"Pro-collagenase-1 (matrix metalloproteinase-1) binds the alpha(2)beta(1) integrin upon release from keratinocytes migrating on type I collagen"
609:
2132:
1549:
834:"Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed beta-propeller"
1819:
1783:
2491:
1175:"Chromatin insulation orchestrates matrix metalloproteinase gene cluster expression reprogramming in aggressive breast cancer tumors"
2185:
960:
Maskos K, Bode W (November 2003). "Structural basis of matrix metalloproteinases and tissue inhibitors of metalloproteinases".
1776:
1327:
Massova I, Kotra LP, Fridman R, Mobashery S (1998). "Matrix metalloproteinases: structures, evolution, and diversification".
2341:
1310:
Krane SM (1995). "Is collagenase (matrix metalloproteinase-1) necessary for bone and other connective tissue remodeling?".
2456:
769:"Human fibroblast collagenase. Complete primary structure and homology to an oncogene transformation-induced rat protein"
2137:
556:
832:
Li J, Brick P, O'Hare MC, Skarzynski T, Lloyd LF, Curry VA, Clark IM, Bigg HF, Hazleman BL, Cawston TE (June 1995).
2031:
2026:
2326:
2442:
2429:
2416:
2403:
2390:
2377:
2364:
1810:
1542:
1226:"Structural analysis of the alpha(2) integrin I domain/procollagenase-1 (matrix metalloproteinase-1) interaction"
2336:
1728:: CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH CGS-27023A, NMR, MINIMIZED AVERAGE STRUCTURE
2290:
2233:
2147:
1964:
1807:
479:
2238:
1758:: CRYSTAL STRUCTURE OF FIBROBLAST COLLAGENASE-1 COMPLEXED TO A DIPHENYL-ETHER SULPHONE BASED HYDROXAMIC ACID
468:
1336:
1265:
Dumin JA, Dickeson SK, Stricker TP, Bhattacharyya-Pakrasi M, Roby JD, Santoro SA, Parks WC (August 2001).
2259:
2178:
2122:
2331:
623:"Molecular cloning of human synovial cell collagenase and selection of a single gene from genomic DNA"
2486:
1803:
1668:: INHIBITOR-FREE CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE, NMR, MINIMIZED AVERAGE STRUCTURE
1535:
718:
536:
483:
1698:: CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF MMP-1 IN COMPLEX WITH THE INHIBITORY DOMAIN OF TIMP-1
579:
2295:
1341:
1743:: CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH CGS-27023A, NMR, 30 STRUCTURES
2496:
2228:
1070:
985:
942:
55:
1768:
1713:: STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH AN INHIBITOR
808:
1504:
1474:
1439:
1410:
1389:
1354:
1315:
1288:
1247:
1206:
1155:
1119:
1062:
1026:
977:
934:
896:
855:
790:
746:
687:
652:
405:
34:
1422:
Seiki M (2003). "Membrane-type 1 matrix metalloproteinase: a key enzyme for tumor invasion".
2274:
2269:
2243:
2171:
2071:
1464:
1431:
1379:
1346:
1278:
1237:
1196:
1186:
1147:
1109:
1101:
1054:
1016:
969:
926:
886:
845:
780:
736:
726:
679:
642:
634:
451:
421:
1608:: CRYSTAL STRUCTURES OF RECOMBINANT 19-KDA HUMAN FIBROBLAST COLLAGENASE COMPLEXED TO ITSELF
1593:: CRYSTAL STRUCTURES OF RECOMBINANT 19-KDA HUMAN FIBROBLAST COLLAGENASE COMPLEXED TO ITSELF
1498:
1224:
Stricker TP, Dumin JA, Dickeson SK, Chung L, Nagase H, Parks WC, Santoro SA (August 2001).
2321:
2305:
2218:
1827:
519:
1623:: STRUCTURE OF THE CATALYTIC DOMAIN OF FIBROBLAST COLLAGENASE COMPLEXED WITH AN INHIBITOR
1201:
1174:
1173:
Llinà s-Arias P, Ensenyat-Mendez M, Íñiguez-Muñoz S, Orozco J, Valdez B (November 2023).
722:
2470:
2359:
2300:
1578:: INHIBITOR-FREE CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE, NMR, 30 STRUCTURES
1114:
1089:
1088:
Stöcker W, Grams F, Baumann U, Reinemer P, Gomis-Rüth FX, McKay DB, Bode W (May 1995).
1003:
Chung L, Shimokawa K, Dinakarpandian D, Grams F, Fields GB, Nagase H (September 2000).
464:
409:
1435:
850:
833:
785:
768:
741:
706:
647:
622:
52:
2480:
2264:
2223:
1683:: CRYSTAL STRUCTURE OF THE ACTIVE FORM (FULL-LENGTH) OF HUMAN FIBROBLAST COLLAGENASE.
1513:
1151:
1058:
507:
1074:
989:
946:
2213:
515:
428:-like domain. The primary structure of MMP-1 was first published by Goldberg, G I,
891:
874:
2437:
2372:
2208:
2142:
2127:
1972:
767:
Goldberg GI, Wilhelm SM, Kronberger A, Bauer EA, Grant GA, Eisen AZ (May 1986).
401:
2465:
1191:
2117:
1989:
1350:
973:
420:
MMP-1 has an archetypal structure consisting of a pre-domain, a pro-domain, a
1384:
1367:
2411:
2385:
511:
425:
71:
48:
1478:
1443:
1414:
1393:
1292:
1283:
1266:
1251:
1242:
1225:
1210:
1159:
1105:
1030:
1021:
1004:
981:
930:
900:
750:
731:
683:
1638:: 1.56 ANGSTROM STRUCTURE OF MATURE TRUNCATED HUMAN FIBROBLAST COLLAGENASE
1358:
1319:
1123:
1066:
938:
859:
794:
691:
656:
356:
2152:
1954:
1949:
1944:
1799:
1653:: X-ray structure of human proMMP-1: New insights into collagenase action
875:"Matrix metalloproteinases: fold and function of their catalytic domains"
488:
345:
1469:
1452:
621:
Brinckerhoff CE, Ruby PL, Austin SD, Fini ME, White HD (February 1987).
1939:
1934:
1929:
1924:
1919:
1914:
1909:
1518:
1508:
175:
134:
707:"Collagenolytic activity in amphibian tissues: a tissue culture assay"
638:
2424:
2194:
2076:
1904:
1899:
1894:
1889:
1884:
1879:
1874:
1869:
1847:
1842:
1837:
1494:
606:
386:
323:
93:
59:
193:
189:
2398:
2101:
2096:
2091:
2086:
2081:
2066:
2061:
2056:
2051:
2046:
2041:
2036:
2021:
2016:
1864:
1859:
1854:
1832:
560:
544:
497:
2011:
2006:
1999:
1994:
1982:
1977:
540:
396:. The gene is part of a cluster of MMP genes which localize to
393:
2167:
1772:
1531:
1527:
503:
397:
1503:
Overview of all the structural information available in the
404:
both purified to homogeneity as a protein, and cloned as a
2163:
2454:
1497:
online database for peptidases and their inhibitors:
873:
Tallant C, Marrero A, Gomis-RĂĽth FX (January 2010).
2350:
2314:
2283:
2252:
2201:
2110:
1963:
1818:
290:
271:
247:
228:
912:
910:
2179:
1784:
1543:
762:
760:
8:
502:Induction of matrix metalloproteinase 1 in
2186:
2172:
2164:
1791:
1777:
1769:
1550:
1536:
1528:
67:
1468:
1383:
1340:
1282:
1241:
1200:
1190:
1113:
1020:
890:
849:
784:
740:
730:
646:
602:
600:
2461:
1565:
571:
15:
2133:Pregnancy-associated plasma protein A
7:
1517:(Interstitial collagenase) at the
446:Overall structural characteristics
287:
268:
244:
225:
203:
180:
156:
139:
115:
98:
14:
1451:Golubkov VS, Strongin AY (2007).
1401:Okada Y, Hashimoto G (2001). "".
705:Gross J, Lapiere CM (June 1962).
482:are involved in the breakdown of
389:that in humans is encoded by the
2464:
1748:
1733:
1718:
1703:
1688:
1673:
1658:
1643:
1628:
1613:
1598:
1583:
1568:
1453:"Proteolysis-driven oncogenesis"
1152:10.1111/j.1600-0722.2008.00552.x
400:MMP-1 was the first vertebrate
1366:Nagase H, Woessner JF (1999).
1:
1436:10.1016/S0304-3835(02)00699-7
851:10.1016/S0969-2126(01)00188-5
786:10.1016/S0021-9258(19)84605-7
2138:Bone morphogenetic protein 1
1059:10.1016/0014-5793(93)80312-I
892:10.1016/j.bbamcr.2009.04.003
711:Proc. Natl. Acad. Sci. U.S.A
1368:"Matrix metalloproteinases"
522:(a). Reviglio et al., 2003.
2513:
1192:10.1186/s12943-023-01906-8
379:matrix metalloproteinase-1
2492:Matrix metalloproteinases
2342:Michaelis–Menten kinetics
1965:Matrix metalloproteinases
1563:
1351:10.1142/S0217984998001256
1312:Clin. Orthop. Relat. Res.
408:. MMP-1 has an estimated
360:
355:
351:
344:
322:
307:
294:
275:
264:
251:
232:
221:
210:
206:
187:
183:
174:
163:
159:
146:
142:
133:
122:
118:
105:
101:
92:
77:
70:
66:
46:
43:
39:
32:
27:
23:
18:
2234:Diffusion-limited enzyme
2148:Insulin-degrading enzyme
1385:10.1074/jbc.274.31.21491
491:, types I, II, and III.
424:, a linker region and a
371:Interstitial collagenase
19:interstitial collagenase
555:MMP1 has been shown to
1284:10.1074/jbc.M104179200
1243:10.1074/jbc.M102217200
1106:10.1002/pro.5560040502
1022:10.1074/jbc.M004039200
931:10.1002/prot.340190203
879:Biochim. Biophys. Acta
732:10.1073/pnas.48.6.1014
684:10.1006/geno.1996.0557
523:
375:fibroblast collagenase
2327:Eadie–Hofstee diagram
2260:Allosteric regulation
2123:Procollagen peptidase
1804:metalloendopeptidases
501:
469:Metzincin superfamily
2337:Lineweaver–Burk plot
518:(b,c,d) compared to
484:extracellular matrix
1470:10.4161/cc.6.2.3706
974:10.1385/MB:25:3:241
723:1962PNAS...48.1014G
398:chromosome 11q22.3.
2296:Enzyme superfamily
2229:Enzyme promiscuity
1335:(25n26): 1075–95.
524:
2452:
2451:
2161:
2160:
1766:
1765:
639:10.1172/JCI112845
537:insulator element
528:
527:
368:
367:
364:
363:
340:
339:
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302:
284:
283:
260:
259:
241:
240:
217:
216:
200:
199:
170:
169:
153:
152:
129:
128:
112:
111:
2504:
2469:
2468:
2460:
2332:Hanes–Woolf plot
2275:Enzyme activator
2270:Enzyme inhibitor
2244:Enzyme catalysis
2188:
2181:
2174:
2165:
1828:Alpha secretases
1793:
1786:
1779:
1770:
1752:
1737:
1722:
1707:
1692:
1677:
1662:
1647:
1632:
1617:
1602:
1587:
1572:
1552:
1545:
1538:
1529:
1482:
1472:
1447:
1418:
1397:
1387:
1362:
1344:
1323:
1297:
1296:
1286:
1277:(31): 29368–74.
1262:
1256:
1255:
1245:
1236:(31): 29375–81.
1221:
1215:
1214:
1204:
1194:
1179:Molecular Cancer
1170:
1164:
1163:
1140:Eur. J. Oral Sci
1134:
1128:
1127:
1117:
1085:
1079:
1078:
1041:
1035:
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1024:
1000:
994:
993:
957:
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914:
905:
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894:
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853:
829:
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696:
695:
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650:
618:
612:
604:
595:
594:
592:
590:
576:
539:located between
520:artificial tears
494:
493:
452:catalytic domain
437:Catalytic domain
422:catalytic domain
373:, also known as
353:
352:
336:
331:
318:
313:
298:
288:
279:
269:
265:RefSeq (protein)
255:
245:
236:
226:
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181:
157:
140:
116:
99:
68:
62:
37:
16:
2512:
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2505:
2503:
2502:
2501:
2477:
2476:
2475:
2463:
2455:
2453:
2448:
2360:Oxidoreductases
2346:
2322:Enzyme kinetics
2310:
2306:List of enzymes
2279:
2248:
2219:Catalytic triad
2197:
2192:
2162:
2157:
2106:
1959:
1814:
1797:
1767:
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1759:
1753:
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1714:
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1588:
1579:
1573:
1559:
1556:
1525:
1490:
1485:
1450:
1421:
1409:(11): 1309–21.
1400:
1378:(31): 21491–4.
1365:
1326:
1309:
1305:
1303:Further reading
1300:
1264:
1263:
1259:
1223:
1222:
1218:
1172:
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1136:
1135:
1131:
1087:
1086:
1082:
1053:(1–2): 134–40.
1043:
1042:
1038:
1015:(38): 29610–7.
1002:
1001:
997:
962:Mol. Biotechnol
959:
958:
954:
916:
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871:
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627:J. Clin. Invest
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586:
584:www.uniprot.org
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357:View/Edit Human
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308:Location (UCSC)
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2284:Classification
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2267:
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2256:
2254:
2250:
2249:
2247:
2246:
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2226:
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2216:
2211:
2205:
2203:
2199:
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2183:
2176:
2168:
2159:
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2156:
2155:
2150:
2145:
2140:
2135:
2130:
2125:
2120:
2114:
2112:
2108:
2107:
2105:
2104:
2099:
2094:
2089:
2084:
2079:
2074:
2069:
2064:
2059:
2054:
2049:
2044:
2039:
2034:
2029:
2024:
2019:
2014:
2009:
2004:
2003:
2002:
1997:
1987:
1986:
1985:
1980:
1969:
1967:
1961:
1960:
1958:
1957:
1952:
1947:
1942:
1937:
1932:
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1917:
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1857:
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1773:
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1724:
1717:
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1489:
1488:External links
1486:
1484:
1483:
1448:
1419:
1398:
1363:
1342:10.1.1.31.3959
1324:
1314:(313): 47–53.
1306:
1304:
1301:
1299:
1298:
1257:
1216:
1165:
1129:
1080:
1036:
995:
952:
906:
865:
824:
813:www.ptglab.com
800:
779:(14): 6600–5.
756:
717:(6): 1014–22.
697:
662:
613:
596:
570:
568:
565:
552:
549:
532:
529:
526:
525:
476:
473:
447:
444:
438:
435:
417:
414:
410:molecular mass
366:
365:
362:
361:
359:
349:
348:
342:
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338:
337:
332:
327:
320:
319:
314:
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285:
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273:
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185:
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137:
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102:
96:
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63:
45:
41:
40:
38:
30:
29:
25:
24:
21:
20:
13:
10:
9:
6:
4:
3:
2:
2509:
2498:
2495:
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2484:
2482:
2472:
2467:
2462:
2458:
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2427:
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2414:
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2330:
2328:
2325:
2323:
2320:
2319:
2317:
2313:
2307:
2304:
2302:
2301:Enzyme family
2299:
2297:
2294:
2292:
2289:
2288:
2286:
2282:
2276:
2273:
2271:
2268:
2266:
2265:Cooperativity
2263:
2261:
2258:
2257:
2255:
2251:
2245:
2242:
2240:
2237:
2235:
2232:
2230:
2227:
2225:
2224:Oxyanion hole
2222:
2220:
2217:
2215:
2212:
2210:
2207:
2206:
2204:
2200:
2196:
2189:
2184:
2182:
2177:
2175:
2170:
2169:
2166:
2154:
2151:
2149:
2146:
2144:
2141:
2139:
2136:
2134:
2131:
2129:
2126:
2124:
2121:
2119:
2116:
2115:
2113:
2109:
2103:
2100:
2098:
2095:
2093:
2090:
2088:
2085:
2083:
2080:
2078:
2075:
2073:
2070:
2068:
2065:
2063:
2060:
2058:
2055:
2053:
2050:
2048:
2045:
2043:
2040:
2038:
2035:
2033:
2030:
2028:
2025:
2023:
2020:
2018:
2015:
2013:
2010:
2008:
2005:
2001:
1998:
1996:
1993:
1992:
1991:
1988:
1984:
1981:
1979:
1976:
1975:
1974:
1971:
1970:
1968:
1966:
1962:
1956:
1953:
1951:
1948:
1946:
1943:
1941:
1938:
1936:
1933:
1931:
1928:
1926:
1923:
1921:
1918:
1916:
1913:
1911:
1908:
1906:
1903:
1901:
1898:
1896:
1893:
1891:
1888:
1886:
1883:
1881:
1878:
1876:
1873:
1871:
1868:
1866:
1863:
1861:
1858:
1856:
1853:
1849:
1846:
1844:
1841:
1839:
1836:
1834:
1831:
1830:
1829:
1826:
1825:
1823:
1821:
1820:ADAM proteins
1817:
1812:
1809:
1805:
1801:
1794:
1789:
1787:
1782:
1780:
1775:
1774:
1771:
1757:
1751:
1746:
1742:
1736:
1731:
1727:
1721:
1716:
1712:
1706:
1701:
1697:
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1667:
1661:
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1646:
1641:
1637:
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1596:
1592:
1586:
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1577:
1571:
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1553:
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1541:
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1530:
1526:
1520:
1516:
1515:
1510:
1506:
1502:
1500:
1496:
1492:
1491:
1487:
1480:
1476:
1471:
1466:
1463:(2): 147–50.
1462:
1458:
1454:
1449:
1445:
1441:
1437:
1433:
1429:
1425:
1420:
1416:
1412:
1408:
1404:
1399:
1395:
1391:
1386:
1381:
1377:
1373:
1372:J. Biol. Chem
1369:
1364:
1360:
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1338:
1334:
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1317:
1313:
1308:
1307:
1302:
1294:
1290:
1285:
1280:
1276:
1272:
1271:J. Biol. Chem
1268:
1261:
1258:
1253:
1249:
1244:
1239:
1235:
1231:
1230:J. Biol. Chem
1227:
1220:
1217:
1212:
1208:
1203:
1198:
1193:
1188:
1184:
1180:
1176:
1169:
1166:
1161:
1157:
1153:
1149:
1146:(4): 319–23.
1145:
1141:
1133:
1130:
1125:
1121:
1116:
1111:
1107:
1103:
1100:(5): 823–40.
1099:
1095:
1091:
1084:
1081:
1076:
1072:
1068:
1064:
1060:
1056:
1052:
1048:
1040:
1037:
1032:
1028:
1023:
1018:
1014:
1010:
1009:J. Biol. Chem
1006:
999:
996:
991:
987:
983:
979:
975:
971:
968:(3): 241–66.
967:
963:
956:
953:
948:
944:
940:
936:
932:
928:
925:(2): 98–109.
924:
920:
913:
911:
907:
902:
898:
893:
888:
884:
880:
876:
869:
866:
861:
857:
852:
847:
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835:
828:
825:
814:
810:
804:
801:
796:
792:
787:
782:
778:
774:
773:J. Biol. Chem
770:
763:
761:
757:
752:
748:
743:
738:
733:
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724:
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708:
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677:
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628:
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617:
614:
611:
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581:
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572:
566:
564:
562:
558:
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548:
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542:
538:
530:
521:
517:
513:
509:
508:ciprofloxacin
505:
500:
496:
495:
492:
490:
485:
481:
474:
472:
470:
466:
465:hydrogen bond
460:
456:
453:
445:
443:
436:
434:
431:
427:
423:
415:
413:
411:
407:
403:
399:
395:
392:
388:
384:
380:
376:
372:
358:
354:
350:
347:
343:
333:
328:
325:
321:
315:
310:
306:
299:
293:
289:
286:
280:
274:
270:
267:
263:
256:
250:
246:
243:
237:
231:
227:
224:
222:RefSeq (mRNA)
220:
213:
209:
205:
202:
196:
195:
191:
186:
182:
179:
177:
173:
166:
162:
158:
155:
149:
145:
141:
138:
136:
132:
125:
121:
117:
114:
108:
104:
100:
97:
95:
91:
88:
85:
83:
80:
76:
73:
69:
65:
61:
57:
53:
50:
42:
36:
31:
26:
22:
17:
2438:Translocases
2435:
2422:
2409:
2396:
2383:
2373:Transferases
2370:
2357:
2214:Binding site
1973:Collagenases
1755:
1740:
1725:
1710:
1695:
1680:
1665:
1650:
1635:
1620:
1605:
1590:
1575:
1524:
1512:
1460:
1456:
1427:
1423:
1406:
1402:
1375:
1371:
1332:
1328:
1311:
1274:
1270:
1260:
1233:
1229:
1219:
1182:
1178:
1168:
1143:
1139:
1132:
1097:
1093:
1083:
1050:
1046:
1039:
1012:
1008:
998:
965:
961:
955:
922:
918:
882:
878:
868:
844:(6): 541–9.
841:
837:
827:
816:. Retrieved
812:
809:"26585-1-AP"
803:
776:
772:
714:
710:
700:
678:(2): 266–8.
675:
671:
665:
633:(2): 542–6.
630:
626:
616:
587:. Retrieved
583:
574:
554:
551:Interactions
534:
516:levofloxacin
478:
461:
457:
449:
440:
429:
419:
390:
382:
378:
374:
370:
369:
295:
276:
252:
233:
211:
188:
164:
147:
123:
106:
86:
81:
44:External IDs
2487:Human genes
2209:Active site
2143:Lysostaphin
2128:Thermolysin
1990:Gelatinases
1558:PDB gallery
1430:(1): 1–11.
1424:Cancer Lett
1094:Protein Sci
885:(1): 20–8.
506:corneas by
412:of 54 kDa.
402:collagenase
60:- orthologs
28:Identifiers
2481:Categories
2412:Isomerases
2386:Hydrolases
2253:Regulation
2118:Neprilysin
1457:Cell Cycle
1185:(4): 190.
818:2021-10-05
607:EntrezGene
567:References
531:Regulation
2497:EC 3.4.24
2291:EC number
1800:Proteases
1403:Seikagaku
1337:CiteSeerX
1047:FEBS Lett
838:Structure
580:"UniProt"
512:ofloxacin
489:collagens
426:hemopexin
416:Structure
385:), is an
72:Orthologs
49:GeneCards
2315:Kinetics
2239:Cofactor
2202:Activity
2153:ZMPSTE24
1955:ADAMTS13
1950:ADAMTS12
1945:ADAMTS10
1479:17245132
1444:12706853
1415:11831026
1394:10419448
1293:11359786
1252:11359774
1211:38017545
1202:10683115
1160:18705799
1075:27244239
1031:10871619
990:24110599
982:14668538
947:23973090
919:Proteins
901:19374923
751:13902219
672:Genomics
557:interact
475:Function
346:Wikidata
2471:Biology
2425:Ligases
2195:Enzymes
1940:ADAMTS9
1935:ADAMTS8
1930:ADAMTS5
1925:ADAMTS4
1920:ADAMTS3
1915:ADAMTS2
1910:ADAMTS1
1519:PDBe-KB
1509:UniProt
1499:M10.001
1359:9737711
1329:FASEB J
1320:7641497
1124:7663339
1115:2143131
1067:8405391
939:8090713
860:8590015
795:3009463
719:Bibcode
692:8921407
657:3027129
589:17 July
547:genes.
176:UniProt
135:Ensembl
78:Species
35:Aliases
2457:Portal
2399:Lyases
2077:MMP23B
2072:MMP23A
1905:ADAM33
1900:ADAM28
1895:ADAM23
1890:ADAM22
1885:ADAM18
1880:ADAM15
1875:ADAM12
1870:ADAM11
1848:ADAM19
1843:ADAM17
1838:ADAM10
1811:3.4.24
1514:P03956
1495:MEROPS
1477:
1442:
1413:
1392:
1357:
1339:
1318:
1291:
1250:
1209:
1199:
1158:
1122:
1112:
1073:
1065:
1029:
988:
980:
945:
937:
899:
858:
793:
749:
742:220898
739:
690:
655:
648:424122
645:
430:et al.
387:enzyme
326:search
324:PubMed
94:Entrez
2351:Types
2111:Other
2102:MMP28
2097:MMP27
2092:MMP26
2087:MMP25
2082:MMP24
2067:MMP21
2062:MMP20
2057:MMP19
2052:MMP17
2047:MMP16
2042:MMP15
2037:MMP14
2032:MMP13
2027:MMP12
2022:MMP11
2017:MMP10
1865:ADAM8
1860:ADAM7
1855:ADAM2
1833:ADAM9
1071:S2CID
986:S2CID
943:S2CID
561:CD49b
559:with
545:MMP10
383:MMP-1
377:and
87:Mouse
82:Human
2443:list
2436:EC7
2430:list
2423:EC6
2417:list
2410:EC5
2404:list
2397:EC4
2391:list
2384:EC3
2378:list
2371:EC2
2365:list
2358:EC1
2012:MMP7
2007:MMP3
2000:MMP9
1995:MMP2
1983:MMP8
1978:MMP1
1756:966c
1741:4ayk
1726:3ayk
1711:2tcl
1696:2j0t
1681:2clt
1666:2ayk
1651:1su3
1636:1hfc
1621:1cgl
1606:1cgf
1591:1cge
1576:1ayk
1507:for
1493:The
1475:PMID
1440:PMID
1411:PMID
1390:PMID
1355:PMID
1316:PMID
1289:PMID
1248:PMID
1207:PMID
1156:PMID
1120:PMID
1063:PMID
1027:PMID
978:PMID
935:PMID
897:PMID
883:1803
856:PMID
791:PMID
747:PMID
688:PMID
653:PMID
610:4312
591:2022
543:and
541:MMP8
514:and
480:MMPs
450:The
406:cDNA
394:gene
391:MMP1
1505:PDB
1465:doi
1432:doi
1428:194
1380:doi
1376:274
1347:doi
1279:doi
1275:276
1238:doi
1234:276
1197:PMC
1187:doi
1148:doi
1144:116
1110:PMC
1102:doi
1055:doi
1051:331
1017:doi
1013:275
970:doi
927:doi
887:doi
846:doi
781:doi
777:261
737:PMC
727:doi
680:doi
643:PMC
635:doi
504:rat
335:n/a
330:n/a
317:n/a
312:n/a
297:n/a
278:n/a
254:n/a
235:n/a
212:n/a
165:n/a
148:n/a
124:n/a
107:n/a
56:OMA
2483::
1808:EC
1802::
1511::
1473:.
1459:.
1455:.
1438:.
1426:.
1407:73
1405:.
1388:.
1374:.
1370:.
1353:.
1345:.
1333:12
1331:.
1287:.
1273:.
1269:.
1246:.
1232:.
1228:.
1205:.
1195:.
1183:22
1181:.
1177:.
1154:.
1142:.
1118:.
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1096:.
1092:.
1069:.
1061:.
1049:.
1025:.
1011:.
1007:.
984:.
976:.
966:25
964:.
941:.
933:.
923:19
921:.
909:^
895:.
881:.
877:.
854:.
840:.
836:.
811:.
789:.
775:.
771:.
759:^
745:.
735:.
725:.
715:48
713:.
709:.
686:.
676:37
674:.
651:.
641:.
631:79
629:.
625:.
599:^
582:.
563:.
510:,
54:;
51::
2459::
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2441:(
2432:)
2428:(
2419:)
2415:(
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2402:(
2393:)
2389:(
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2376:(
2367:)
2363:(
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1551:e
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1481:.
1467::
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1150::
1126:.
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1033:.
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992:.
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929::
903:.
889::
862:.
848::
842:3
821:.
797:.
783::
753:.
729::
721::
694:.
682::
659:.
637::
593:.
381:(
194:a
190:n
58::
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