426:-like in-line displacement mechanism has been proposed. In this mechanism, both PAPS and the target tyrosine bind to the same active site in the enzyme and are orientated in a way such that a glutamic acid residue acts as a catalytic base on the tyrosine hydroxyl group, an arginine residue acts as a catalytic acid, and serine and lysine residues are used to stabilize the SN2-like intermediate. The deprotonated hydroxyl would attack the sulfonate group, then displace the phosphate group and PAP would be released, along with the sulfotyrosine residue.
249:
257:
47:
1847:
367:. It consists of a short cytosolic region that contains the N-terminus of the protein, a single transmembrane region of about 17 amino acids in length, a small stem region of about 40 amino acids in length, and a larger, catalytic region that is located on the luminal side of the membrane. It is localized to the
413:
for TPST and the tyrosine sulfating has been proposed. PAPS enters one site of TPST and the sulfonate group is transferred to a
Histidine residue in the enzyme and PAP is released. Then, the target protein and tyrosine bind TPST and the histidine transfers the sulfonate group to the target tyrosine.
298:
TPST and tyrosine sulfation is involved in a large number of biological and physiological processes. Tyrosine sulfation has been found to be an important part of the inflammatory process, leukocyte movement and cytosis, viral cell entrance, and other cell-cell and protein-protein interactions.
379:
in mammals, TPST-1 and TPST-2, that are 370 and 377 residues in length, respectively. Both are quite similar with an approximately 63% amino acid identity, but show slightly different protein substrate specificities.
1385:
303:(PSGL-1) has been extensively studied as a substrate for TPST and the importance of sulfation in PSGL-1 and its ability to bind its receptor. Another substrate for TPST, CC-chemokine Receptor 5 (
1081:"Tyrosylprotein sulfotransferase: purification and molecular cloning of an enzyme that catalyzes tyrosine O-sulfation, a common posttranslational modification of eukaryotic proteins"
311:
invasion has led to research on TPST and CCR5, including a characterization of the pattern of sulfation of CCR5. Beyond these two proteins, other notable protein substrates include
1378:
295:
donor and binds proteins with target tyrosine residues to eventually form the tyrosine O-sulfate ester group and the desulfonated 3’-phosphoadenosine-5’-phosphate (PAP).
212:
1371:
617:
464:
383:
TPST is a prevalent enzyme, found in many multicellular eukaryotes including mammals, most vertebrates, and a number of invertebrate species as well, including
299:
Selection for specific tyrosine residues requires a generally accessible tyrosine residue, and acidic residues within +5 or -5 residues of the target tyrosine.
231:
828:
Stone MJ, Chuang S, Hou X, Shoham M, Zhu JZ (Jun 2009). "Tyrosine sulfation: an increasingly recognised post-translational modification of secreted proteins".
916:
Teramoto T, Fujikawa Y, Kawaguchi Y, Kurogi K, Soejima M, Adachi R, Nakanishi Y, Mishiro-Sato E, Liu MC, Sakakibara Y, Suiko M, Kimura M, Kakuta Y (2013).
288:
1450:
307:), has generated interest because of its role as the target protein for the viral entrance of HIV into cells. The importance of CCR5's sulfation for
1440:
389:. Its importance can be further demonstrated by the fact as much as 1% of all secreted and membrane tyrosine residues are found to be sulfated.
1872:
375:-Golgi region, and acts almost exclusively on secretory and plasma membrane proteins. TPST is about 50-54 kD in size, and has two confirmed
340:
1019:"Tyrosine sulfation of CCR5 N-terminal peptide by tyrosylprotein sulfotransferases 1 and 2 follows a discrete pattern and temporal sequence"
397:
Within the last two years, using the crystallized structure of the catalytic region of TPST-2 and different experiments other methods using
1867:
1533:
1435:
641:
488:
1566:
629:
476:
300:
224:
284:
1256:
Chen BH, Wang CC, Lu LY, Hung KS, Yang YS (Feb 2013). "Fluorescence assay for protein post-translational tyrosine sulfation".
1199:"Existence of distinct tyrosylprotein sulfotransferase genes: molecular characterization of tyrosylprotein sulfotransferase-2"
622:
469:
175:
151:
1722:
918:"Crystal structure of human tyrosylprotein sulfotransferase-2 reveals the mechanism of protein tyrosine sulfation reaction"
1423:
1837:
776:"Tyrosine-O-sulfated proteins of PC12 pheochromocytoma cells and their sulfation by a tyrosylprotein sulfotransferase"
348:
1197:
Beisswanger R, Corbeil D, Vannier C, Thiele C, Dohrmann U, Kellner R, Ashman K, Niehrs C, Huttner WB (Sep 15, 1998).
1514:
1707:
1823:
1810:
1797:
1784:
1771:
1758:
1745:
1524:
1502:
1470:
1411:
31:
1717:
169:
1671:
1614:
1482:
1402:
1357:
682:
529:
62:
1140:"(Glu62, Ala30, Tyr8) n serves as high-affinity substrate for tyrosylprotein sulfotransferase: a Golgi enzyme"
1304:"Catalytic mechanism of Golgi-resident human tyrosylprotein sulfotransferase-2: a mass spectrometry approach"
156:
1619:
385:
1353:
1445:
634:
481:
336:
236:
1640:
1559:
1492:
699:
364:
144:
1712:
248:
256:
79:
1460:
1210:
1151:
1092:
1030:
929:
546:
1676:
410:
172:
74:
96:
1609:
1363:
1281:
268:
872:
Niehrs C, Beisswanger R, Huttner WB (Jun 1994). "Protein tyrosine sulfation, 1993--an update".
1877:
1415:
1333:
1273:
1238:
1179:
1120:
1058:
996:
955:
889:
845:
797:
398:
163:
1655:
1650:
1624:
1552:
1474:
1323:
1315:
1265:
1228:
1218:
1169:
1159:
1110:
1100:
1048:
1038:
986:
945:
937:
881:
837:
787:
755:
703:
694:
550:
541:
687:
534:
132:
1702:
1686:
1599:
1455:
723:
570:
368:
312:
51:
An image of a single subunit of the catalytic region of TPST-2 from protein structure 3AP1
352:
108:
1214:
1155:
1096:
1034:
933:
67:
46:
1851:
1740:
1681:
1328:
1303:
950:
917:
207:
1174:
1139:
1053:
1018:
991:
974:
792:
775:
187:
1861:
1645:
1604:
1285:
1233:
1198:
1115:
1080:
885:
182:
260:
A model for a proposed SN2-like In-Line
Displacement mechanism of Tyrosine Sulfation
1594:
423:
658:
505:
1818:
1753:
1589:
1394:
1319:
733:
580:
320:
191:
1846:
1203:
Proceedings of the
National Academy of Sciences of the United States of America
1144:
Proceedings of the
National Academy of Sciences of the United States of America
1085:
Proceedings of the
National Academy of Sciences of the United States of America
1023:
Proceedings of the
National Academy of Sciences of the United States of America
975:"Tyrosine sulfation: a modulator of extracellular protein-protein interactions"
1506:
1269:
841:
665:
512:
332:
1223:
1792:
1766:
1428:
1164:
344:
292:
280:
1337:
1277:
1105:
1062:
1043:
1000:
959:
849:
434:
Human genes that encode protein-tyrosine sulfotransferase enzymes include:
1242:
1183:
1124:
893:
801:
670:
517:
316:
120:
941:
376:
328:
324:
252:
A model for a proposed 2-Site Ping-Pong mechanism of
Tyrosine Sulfation
139:
1805:
1575:
1398:
653:
500:
219:
115:
103:
91:
17:
422:
Based on crystal structure of TPST-2 with C4 complement and PAP, an
1017:
Seibert C, Cadene M, Sanfiz A, Chait BT, Sakmar TP (Aug 20, 2002).
1779:
610:
457:
255:
247:
1302:
Danan LM, Yu Z, Ludden PJ, Jia W, Moore KL, Leary JA (Sep 2010).
279:
Tyrosylprotein sulfotransferase is the enzyme that catalyzes the
646:
493:
304:
127:
1548:
1367:
308:
1544:
30:"TPST" redirects here. For the switch configuration, see
401:
methods have come to propose two separate mechanisms.
1835:
1308:
Journal of the
American Society for Mass Spectrometry
363:
Tyrosylprotein sulfotransferase (TPST) is a type II
1731:
1695:
1664:
1633:
1582:
1523:
1501:
1469:
1410:
729:
719:
714:
693:
681:
676:
664:
652:
640:
628:
616:
606:
601:
596:
576:
566:
561:
540:
528:
523:
511:
499:
487:
475:
463:
453:
448:
443:
230:
218:
206:
201:
181:
162:
150:
138:
126:
114:
102:
90:
85:
73:
61:
56:
39:
1297:
1295:
1012:
1010:
911:
909:
907:
905:
903:
823:
821:
819:
817:
815:
813:
811:
1560:
1379:
1079:Ouyang Yb, Lane WS, Moore KL (Mar 17, 1998).
1074:
1072:
867:
865:
863:
861:
859:
8:
1567:
1553:
1545:
1386:
1372:
1364:
711:
558:
351:. A full, up-to-date list can be found at
198:
45:
1356:at the U.S. National Library of Medicine
1327:
1232:
1222:
1173:
1163:
1114:
1104:
1052:
1042:
990:
949:
791:
1842:
766:
418:SN2-like in-line displacement mechanism
1258:Analytical and Bioanalytical Chemistry
593:
440:
36:
1451:thiosulfate—dithiol sulfurtransferase
774:Lee RW, Huttner WB (September 1983).
341:follicle-stimulating hormone receptor
289:3'-Phosphoadenosine-5'-phosphosulfate
7:
1534:Coenzyme-B sulfoethylthiotransferase
1436:3-mercaptopyruvate sulfurtransferase
1441:thiosulfate—thiol sulfurtransferase
973:Kehoe JW, Bertozzi CR (Mar 2000).
25:
597:tyrosylprotein sulfotransferase 2
444:tyrosylprotein sulfotransferase 1
283:reaction of protein tyrosines, a
1845:
301:P-selectin glycoprotein ligand-1
1488:Tyrosylprotein sulfotransferase
1354:tyrosylprotein+sulfotransferase
1138:Lee RW, Huttner WB (Sep 1985).
874:Chemico-Biological Interactions
359:Characterization and properties
285:post-translational modification
265:Tyrosylprotein sulfotransferase
40:Tyrosylprotein sulfotransferase
1:
1424:Thiosulfate sulfurtransferase
992:10.1016/s1074-5521(00)00093-4
793:10.1016/S0021-9258(17)44421-8
1873:Genes on human chromosome 22
886:10.1016/0009-2797(94)90068-x
405:Two-site ping-pong mechanism
267:is an enzyme that catalyzes
1868:Genes on human chromosome 7
1320:10.1016/j.jasms.2010.03.037
349:G-protein coupled receptors
1894:
1515:Propionate CoA-transferase
29:
1723:Michaelis–Menten kinetics
1270:10.1007/s00216-012-6540-3
842:10.1016/j.nbt.2009.03.011
710:
557:
287:of proteins. It utilizes
197:
44:
32:Triple pole, single throw
1615:Diffusion-limited enzyme
1483:Alcohol sulfotransferase
1358:Medical Subject Headings
1224:10.1073/pnas.95.19.11134
1165:10.1073/pnas.82.18.6143
979:Chemistry & Biology
386:Drosophila melanogaster
1446:tRNA sulfurtransferase
1106:10.1073/pnas.95.6.2896
1044:10.1073/pnas.172380899
371:, specifically in the
337:Complement component 4
261:
253:
1708:Eadie–Hofstee diagram
1641:Allosteric regulation
1493:Aryl sulfotransferase
922:Nature Communications
365:transmembrane protein
259:
251:
1718:Lineweaver–Burk plot
1461:cysteine desulfurase
1401:-containing group (
1215:1998PNAS...9511134B
1156:1985PNAS...82.6143L
1097:1998PNAS...95.2896O
1035:2002PNAS...9911031S
934:2013NatCo...4.1572T
411:ping-pong mechanism
327:, the leech enzyme
1677:Enzyme superfamily
1610:Enzyme promiscuity
1416:Sulfurtransferases
942:10.1038/ncomms2593
343:(FSHR), and other
269:tyrosine sulfation
262:
254:
1833:
1832:
1542:
1541:
1475:Sulfotransferases
830:New Biotechnology
747:
746:
743:
742:
739:
738:
590:
589:
586:
585:
399:mass spectrometry
246:
245:
242:
241:
145:metabolic pathway
16:(Redirected from
1885:
1850:
1849:
1841:
1713:Hanes–Woolf plot
1656:Enzyme activator
1651:Enzyme inhibitor
1625:Enzyme catalysis
1569:
1562:
1555:
1546:
1507:CoA-transferases
1388:
1381:
1374:
1365:
1342:
1341:
1331:
1299:
1290:
1289:
1253:
1247:
1246:
1236:
1226:
1194:
1188:
1187:
1177:
1167:
1135:
1129:
1128:
1118:
1108:
1076:
1067:
1066:
1056:
1046:
1014:
1005:
1004:
994:
970:
964:
963:
953:
913:
898:
897:
869:
854:
853:
825:
806:
805:
795:
786:(18): 11326–34.
771:
756:Sulfotransferase
712:
594:
559:
441:
437:
436:
199:
49:
37:
21:
1893:
1892:
1888:
1887:
1886:
1884:
1883:
1882:
1858:
1857:
1856:
1844:
1836:
1834:
1829:
1741:Oxidoreductases
1727:
1703:Enzyme kinetics
1691:
1687:List of enzymes
1660:
1629:
1600:Catalytic triad
1578:
1573:
1543:
1538:
1519:
1497:
1465:
1456:biotin synthase
1406:
1392:
1350:
1345:
1301:
1300:
1293:
1255:
1254:
1250:
1209:(19): 11134–9.
1196:
1195:
1191:
1137:
1136:
1132:
1091:(6): 2896–901.
1078:
1077:
1070:
1029:(17): 11031–6.
1016:
1015:
1008:
972:
971:
967:
915:
914:
901:
880:(1–3): 257–71.
871:
870:
857:
827:
826:
809:
773:
772:
768:
764:
752:
432:
420:
407:
395:
369:Golgi apparatus
361:
313:Cholecystokinin
277:
52:
35:
28:
23:
22:
15:
12:
11:
5:
1891:
1889:
1881:
1880:
1875:
1870:
1860:
1859:
1855:
1854:
1831:
1830:
1828:
1827:
1814:
1801:
1788:
1775:
1762:
1749:
1735:
1733:
1729:
1728:
1726:
1725:
1720:
1715:
1710:
1705:
1699:
1697:
1693:
1692:
1690:
1689:
1684:
1679:
1674:
1668:
1666:
1665:Classification
1662:
1661:
1659:
1658:
1653:
1648:
1643:
1637:
1635:
1631:
1630:
1628:
1627:
1622:
1617:
1612:
1607:
1602:
1597:
1592:
1586:
1584:
1580:
1579:
1574:
1572:
1571:
1564:
1557:
1549:
1540:
1539:
1537:
1536:
1530:
1528:
1521:
1520:
1518:
1517:
1511:
1509:
1499:
1498:
1496:
1495:
1490:
1485:
1479:
1477:
1467:
1466:
1464:
1463:
1458:
1453:
1448:
1443:
1438:
1433:
1432:
1431:
1420:
1418:
1408:
1407:
1393:
1391:
1390:
1383:
1376:
1368:
1362:
1361:
1349:
1348:External links
1346:
1344:
1343:
1314:(9): 1633–42.
1291:
1248:
1189:
1150:(18): 6143–7.
1130:
1068:
1006:
965:
899:
855:
836:(5): 299–317.
807:
765:
763:
760:
759:
758:
751:
748:
745:
744:
741:
740:
737:
736:
731:
727:
726:
721:
717:
716:
708:
707:
697:
691:
690:
685:
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678:
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632:
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608:
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603:
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584:
583:
578:
574:
573:
568:
564:
563:
555:
554:
544:
538:
537:
532:
526:
525:
521:
520:
515:
509:
508:
503:
497:
496:
491:
485:
484:
479:
473:
472:
467:
461:
460:
455:
451:
450:
446:
445:
431:
428:
419:
416:
406:
403:
394:
391:
360:
357:
291:(PAPS) as the
276:
273:
244:
243:
240:
239:
234:
228:
227:
222:
216:
215:
210:
204:
203:
195:
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185:
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167:
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142:
136:
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106:
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99:
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82:
77:
71:
70:
65:
59:
58:
54:
53:
50:
42:
41:
26:
24:
14:
13:
10:
9:
6:
4:
3:
2:
1890:
1879:
1876:
1874:
1871:
1869:
1866:
1865:
1863:
1853:
1848:
1843:
1839:
1825:
1821:
1820:
1815:
1812:
1808:
1807:
1802:
1799:
1795:
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1789:
1786:
1782:
1781:
1776:
1773:
1769:
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1763:
1760:
1756:
1755:
1750:
1747:
1743:
1742:
1737:
1736:
1734:
1730:
1724:
1721:
1719:
1716:
1714:
1711:
1709:
1706:
1704:
1701:
1700:
1698:
1694:
1688:
1685:
1683:
1682:Enzyme family
1680:
1678:
1675:
1673:
1670:
1669:
1667:
1663:
1657:
1654:
1652:
1649:
1647:
1646:Cooperativity
1644:
1642:
1639:
1638:
1636:
1632:
1626:
1623:
1621:
1618:
1616:
1613:
1611:
1608:
1606:
1605:Oxyanion hole
1603:
1601:
1598:
1596:
1593:
1591:
1588:
1587:
1585:
1581:
1577:
1570:
1565:
1563:
1558:
1556:
1551:
1550:
1547:
1535:
1532:
1531:
1529:
1526:
1522:
1516:
1513:
1512:
1510:
1508:
1504:
1500:
1494:
1491:
1489:
1486:
1484:
1481:
1480:
1478:
1476:
1472:
1468:
1462:
1459:
1457:
1454:
1452:
1449:
1447:
1444:
1442:
1439:
1437:
1434:
1430:
1427:
1426:
1425:
1422:
1421:
1419:
1417:
1413:
1409:
1404:
1400:
1396:
1389:
1384:
1382:
1377:
1375:
1370:
1369:
1366:
1359:
1355:
1352:
1351:
1347:
1339:
1335:
1330:
1325:
1321:
1317:
1313:
1309:
1305:
1298:
1296:
1292:
1287:
1283:
1279:
1275:
1271:
1267:
1264:(4): 1425–9.
1263:
1259:
1252:
1249:
1244:
1240:
1235:
1230:
1225:
1220:
1216:
1212:
1208:
1204:
1200:
1193:
1190:
1185:
1181:
1176:
1171:
1166:
1161:
1157:
1153:
1149:
1145:
1141:
1134:
1131:
1126:
1122:
1117:
1112:
1107:
1102:
1098:
1094:
1090:
1086:
1082:
1075:
1073:
1069:
1064:
1060:
1055:
1050:
1045:
1040:
1036:
1032:
1028:
1024:
1020:
1013:
1011:
1007:
1002:
998:
993:
988:
985:(3): R57-61.
984:
980:
976:
969:
966:
961:
957:
952:
947:
943:
939:
935:
931:
927:
923:
919:
912:
910:
908:
906:
904:
900:
895:
891:
887:
883:
879:
875:
868:
866:
864:
862:
860:
856:
851:
847:
843:
839:
835:
831:
824:
822:
820:
818:
816:
814:
812:
808:
803:
799:
794:
789:
785:
781:
780:J. Biol. Chem
777:
770:
767:
761:
757:
754:
753:
749:
735:
732:
728:
725:
722:
718:
713:
709:
706:
705:
701:
698:
696:
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531:
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183:Gene Ontology
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121:NiceZyme view
119:
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55:
48:
43:
38:
33:
19:
1819:Translocases
1816:
1803:
1790:
1777:
1764:
1754:Transferases
1751:
1738:
1595:Binding site
1487:
1395:Transferases
1311:
1307:
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1206:
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1088:
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264:
263:
109:BRENDA entry
1590:Active site
1527:: Alkylthio
724:Swiss-model
602:Identifiers
571:Swiss-model
449:Identifiers
409:A two-site
321:Factor VIII
97:IntEnz view
80:87588-33-8
57:Identifiers
1862:Categories
1793:Isomerases
1767:Hydrolases
1634:Regulation
762:References
720:Structures
715:Search for
677:Other data
567:Structures
562:Search for
524:Other data
333:fibrinogen
166:structures
133:KEGG entry
1672:EC number
1429:Rhodanese
1286:206911254
683:EC number
659:NM_003595
618:NCBI gene
530:EC number
506:NM_003596
465:NCBI gene
393:Mechanism
353:UniProtKB
345:chemokine
293:sulfonate
281:sulfation
86:Databases
1878:EC 2.8.2
1696:Kinetics
1620:Cofactor
1583:Activity
1338:20462768
1278:23161068
1063:12169668
1001:10712936
960:23481380
928:: 1572.
850:19658209
750:See also
734:InterPro
688:2.8.2.20
581:InterPro
535:2.8.2.20
430:Examples
377:isoforms
317:Factor V
275:Function
237:proteins
225:articles
213:articles
170:RCSB PDB
68:2.8.2.20
1852:Biology
1806:Ligases
1576:Enzymes
1329:3088362
1243:9736702
1211:Bibcode
1184:3862121
1152:Bibcode
1125:9501187
1093:Bibcode
1031:Bibcode
951:3601584
930:Bibcode
894:8033259
802:6577005
730:Domains
700:Chr. 22
666:UniProt
577:Domains
513:UniProt
329:hirudin
325:gastrin
315:(CCK),
192:QuickGO
157:profile
140:MetaCyc
75:CAS no.
1838:Portal
1780:Lyases
1399:sulfur
1360:(MeSH)
1336:
1326:
1284:
1276:
1241:
1231:
1182:
1175:391008
1172:
1123:
1113:
1061:
1054:123205
1051:
999:
958:
948:
892:
848:
800:
671:O60704
654:RefSeq
647:603126
607:Symbol
551:q11.21
547:Chr. 7
518:O60507
501:RefSeq
494:603125
454:Symbol
220:PubMed
202:Search
188:AmiGO
176:PDBsum
116:ExPASy
104:BRENDA
92:IntEnz
63:EC no.
27:Enzyme
1732:Types
1525:2.8.4
1503:2.8.3
1471:2.8.2
1412:2.8.1
1282:S2CID
1234:21608
1116:19666
704:q12.1
695:Locus
635:12021
611:TPST2
542:Locus
482:12020
458:TPST1
373:trans
152:PRIAM
18:TPST2
1824:list
1817:EC7
1811:list
1804:EC6
1798:list
1791:EC5
1785:list
1778:EC4
1772:list
1765:EC3
1759:list
1752:EC2
1746:list
1739:EC1
1405:2.8)
1334:PMID
1274:PMID
1239:PMID
1180:PMID
1121:PMID
1059:PMID
997:PMID
956:PMID
890:PMID
846:PMID
798:PMID
642:OMIM
630:HGNC
623:8459
489:OMIM
477:HGNC
470:8460
347:and
319:and
305:CCR5
232:NCBI
173:PDBe
128:KEGG
1324:PMC
1316:doi
1266:doi
1262:405
1229:PMC
1219:doi
1170:PMC
1160:doi
1111:PMC
1101:doi
1049:PMC
1039:doi
987:doi
946:PMC
938:doi
882:doi
838:doi
788:doi
784:258
424:SN2
309:HIV
208:PMC
164:PDB
1864::
1505::
1473::
1414::
1403:EC
1397::
1332:.
1322:.
1312:21
1310:.
1306:.
1294:^
1280:.
1272:.
1260:.
1237:.
1227:.
1217:.
1207:95
1205:.
1201:.
1178:.
1168:.
1158:.
1148:82
1146:.
1142:.
1119:.
1109:.
1099:.
1089:95
1087:.
1083:.
1071:^
1057:.
1047:.
1037:.
1027:99
1025:.
1021:.
1009:^
995:.
981:.
977:.
954:.
944:.
936:.
924:.
920:.
902:^
888:.
878:92
876:.
858:^
844:.
834:25
832:.
810:^
796:.
782:.
778:.
355:.
339:,
335:,
331:,
323:,
271:.
190:/
1840::
1826:)
1822:(
1813:)
1809:(
1800:)
1796:(
1787:)
1783:(
1774:)
1770:(
1761:)
1757:(
1748:)
1744:(
1568:e
1561:t
1554:v
1387:e
1380:t
1373:v
1340:.
1318::
1288:.
1268::
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1221::
1213::
1186:.
1162::
1154::
1127:.
1103::
1095::
1065:.
1041::
1033::
1003:.
989::
983:7
962:.
940::
932::
926:4
896:.
884::
852:.
840::
804:.
790::
34:.
20:)
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