395:
337:-X-Y structure, x and y being any type of amino acid. Collagen can also be found in two different isoforms, either as a homotrimer or a heterotrimer, both of which can be found during different periods of development. Heterotrimers, in particular, play an important role in wound healing, and are the dominant isoform found in the body.
418:
The molecular mass of type I collagen is 300,000 g/mol and assembles in one of two higher order molecular assemblies. It forms a large solid structure formed by strict and non-flexible protein interactions. This large multi-protein structure is crucially held together by mainly hydrogen bonds and the
385:
and must undergo post-translational modifications in order to make the final type I collagen product. The procollagen complex is then modified by different enzyme proteinases which cleave N and C terminal pro-peptides that are present on either side of the molecule. This process occurs outside of the
380:
The creation process of type I Collagen begins with the production and the combination of two separate subunits, called the pro-alpha1(I) and pro-alpha2(I) chains. These pro-alpha chains are encoded by the COL1A1 and COL1A2 genes respectively and when combined produce type I pro-collagen. This
452:(types 1–4): Mutations in COL1alpha 1 and/or COL1alpha2 are known to cause several different types of Osteogenesis Imperfecta with the severity of said diseases being related to the type and frequency of the mutations occurring. For further information on COL1's effect in this disease, see
441:
Vascular type Ehlers-Danlos
Syndrome: Some patients with Vascular type Ehlers-Danlos, which is caused by mutations in COL3alpha1, are known to also have mutations in the COL1alpha1 gene. However the exact associations remain unknown.
332:
Collagen I itself is created by the combination of both a proalpha1 and a proalpha2 chain created by the COL1alpha1 and COL1alpha2 genes respectively. The Col I gene itself takes up a triple-helical conformation due to its
406:
which is caused by its amino acid composition. Its specific domain follows an order of G-X-Y In which the X and Y slots are occupied by any amino acid other than glycine however these slots are typically occupied by both
445:
Athrochalasia type Ehlers-Danlos
Syndrome: This type of Ehlers-Danlos is caused by the mutation of the COL1alpha1 and COL1alpha2 genes, which are responsible for encoding the proalpha1 and proalpha2 chains respectively.
462:: This condition is caused by a mutation in the COL1alpha gene that replaces arginine with cysteine at the 836 protein site. This particular mutation causes the fibrils of type I to vary greatly in size and shape.
321:
of the human body, consisting of around 90% of the body's total collagen in vertebrates. Due to this, it is also the most abundant protein type found in all vertebrates. Type I forms large,
198:
53:
415:, not in any particular order. This specific conformation will end up being repeated and packed into a hexagonal structure in order to form collagen fibrils.
934:
476:
Markers used to measure bone loss are not easily testable. Degradation of type I collagen releases metabolites that can be used to monitor resorption.
438:: This type of Ehlers-Danlos is caused by mutations within the COL1alpha2 gene, which is responsible for encoding the collagen pro-alpha2 chain.
1613:
340:
Type I collagen can be found in a myriad of different places in the body, mainly forming the matrix of connective tissues. It is present in
1618:
1582:
222:
77:
564:
210:
65:
459:
607:"Stepwise proteolytic activation of type I procollagen to collagen within the secretory pathway of tendon fibroblasts in situ"
203:
58:
1592:
927:
1314:
1218:
1193:
1346:
1275:
1213:
1208:
435:
1264:
1223:
1110:
1105:
1100:
1094:
1013:
500:
757:
1302:
1238:
1181:
1153:
1143:
1073:
1006:
1291:
1026:
988:
920:
495:
490:
471:
453:
386:
cellular membrane at which post processing, the molecules cross link and form a final type I collagen product.
449:
431:
Mutations in genes encoding collagen type 1 are known to cause a myriad of different conditions including:
215:
70:
1360:
382:
123:
955:
268:
1187:
1623:
1526:
1337:
781:
520:
272:
1531:
1341:
1132:
894:
828:
739:
690:
636:
560:
846:
1456:
1451:
1412:
1407:
1402:
1397:
1392:
1137:
1001:
884:
818:
729:
721:
710:"Higher-order assemblies in immune signaling: supramolecular complexes and phase separation"
680:
670:
626:
618:
552:
485:
263:
127:
118:
1577:
1434:
1429:
1424:
1020:
982:
292:
147:
1064:
734:
709:
685:
658:
631:
606:
556:
408:
403:
1607:
1365:
947:
871:
Ting KR, Brady JJ, Hameed A, Le G, Meiller J, Verburgh E, et al. (April 2016).
1489:
873:"Clinical utility of C-terminal telopeptide of type 1 collagen in multiple myeloma"
807:"Mutations in type I collagen genes resulting in osteogenesis imperfecta in humans"
420:
322:
239:
94:
1567:
1496:
1232:
1177:
580:
302:
157:
725:
17:
1198:
394:
357:
353:
246:
101:
349:
329:, which make up most of the rope-like dense connective tissue in the body.
898:
832:
823:
806:
743:
694:
640:
912:
675:
1350:
1329:
966:
318:
251:
106:
549:
Osteogenesis
Imperfecta a Translational Approach to Brittle Bone Disease
1572:
1563:
1511:
1484:
1379:
1355:
1319:
1307:
1125:
1120:
1115:
1043:
943:
622:
412:
345:
334:
889:
872:
1516:
1280:
1253:
1248:
1243:
1168:
1163:
1158:
1148:
1083:
1078:
1036:
1031:
993:
369:
365:
234:
89:
547:
Elena
Makareeva (2014). "Collagen Structure, Folding and Function".
1541:
1536:
1506:
1501:
1479:
1461:
1439:
1048:
1521:
361:
341:
227:
82:
916:
782:"Ehlers Danlos Syndromes - Symptoms, Causes, Treatment | NORD"
419:
fibrils conform to a typical diameter size between 25 - 400
521:"Collagen: What It Is, Types, Function & Benefits"
381:
transcriptional process takes place within the cell's
1556:
1472:
1378:
1328:
1057:
974:
965:
954:
298:
288:
283:
262:
257:
245:
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221:
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176:
171:
153:
143:
138:
117:
112:
100:
88:
76:
64:
52:
44:
39:
34:
758:"Cardiac-Valvular Ehlers-Danlos Syndrome (cvEDS)"
542:
540:
605:Canty-Laird EG, Lu Y, Kadler KE (January 2012).
708:Xia S, Chen Z, Shen C, Fu TM (September 2021).
472:Collagen, type I, alpha 1#Clinical significance
928:
657:Naomi R, Ridzuan PM, Bahari H (August 2021).
8:
652:
650:
971:
962:
935:
921:
913:
423:in this fibril conformation.
280:
135:
888:
822:
733:
684:
674:
630:
393:
659:"Current Insights into Collagen Type I"
512:
168:
31:
398:Chemical Structure of Type I Collagen
7:
29:Type of connective tissue in animals
1583:Cartilage oligomeric matrix protein
853:. U.S. National Library of Medicine
587:. U.S. National Library of Medicine
557:10.1016/B978-0-12-397165-4.00007-1
25:
877:British Journal of Haematology
1:
1614:Genes on human chromosome 17
1347:Cartilage associated protein
1619:Genes on human chromosome 7
501:Collagen, type III, alpha 1
1640:
726:10.1007/s13238-021-00839-6
762:The Ehlers Danlos Society
496:Collagen, type I, alpha 2
491:Collagen, type I, alpha 1
454:Collagen, type 1, alpha 1
279:
172:collagen, type I, alpha 2
134:
35:collagen, type I, alpha 1
811:Acta Biochimica Polonica
805:Gajko-Galicka A (2002).
611:The Biochemical Journal
450:Osteogenesis Imperfecta
427:Implications in Disease
824:10.18388/abp.2002_3802
436:Ehlers-Danlos Syndrome
434:Cardiac Valvular type
402:Type I collagen has a
399:
372:, and organ capsules.
360:, the organic part of
1361:Procollagen peptidase
676:10.3390/polym13162642
466:Clinical significance
397:
383:endoplasmic reticulum
317:is the most abundant
851:MedlinePlus Genetics
585:MedlinePlus Genetics
404:triple-helical form
1527:Matrix gla protein
1338:Prolyl hydroxylase
714:Protein & Cell
623:10.1042/BJ20111379
400:
1601:
1600:
1552:
1551:
1374:
1373:
1342:Lysyl hydroxylase
1133:basement membrane
890:10.1111/bjh.13928
312:
311:
308:
307:
167:
166:
163:
162:
16:(Redirected from
1631:
972:
963:
937:
930:
923:
914:
903:
902:
892:
868:
862:
861:
859:
858:
847:"Caffey disease"
843:
837:
836:
826:
802:
796:
795:
793:
792:
786:rarediseases.org
778:
772:
771:
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595:
593:
592:
577:
571:
570:
544:
535:
534:
532:
531:
525:Cleveland Clinic
517:
486:Type II collagen
325:fibers known as
281:
169:
136:
32:
21:
1639:
1638:
1634:
1633:
1632:
1630:
1629:
1628:
1604:
1603:
1602:
1597:
1548:
1468:
1370:
1324:
1207:transmembrane:
1053:
957:
950:
941:
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906:
870:
869:
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519:
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509:
482:
468:
429:
392:
378:
327:collagen fibers
315:Type I collagen
30:
23:
22:
18:Collagen fibers
15:
12:
11:
5:
1637:
1635:
1627:
1626:
1621:
1616:
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1128:
1123:
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1034:
1029:
1017:
1010:
998:
997:
996:
991:
978:
976:
975:Fibril forming
969:
960:
956:Extracellular
952:
951:
948:scleroproteins
942:
940:
939:
932:
925:
917:
911:
910:
905:
904:
863:
838:
817:(2): 433–441.
797:
773:
749:
720:(9): 680–694.
700:
646:
617:(2): 707–717.
597:
572:
565:
536:
511:
510:
508:
505:
504:
503:
498:
493:
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481:
478:
467:
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460:Caffey Disease
428:
425:
409:hydroxyproline
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1385:
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1381:
1377:
1367:
1366:Lysyl oxidase
1364:
1362:
1359:
1357:
1354:
1352:
1348:
1345:
1343:
1339:
1336:
1335:
1333:
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1318:
1316:
1313:
1309:
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1274:
1273:
1272:
1269:
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1262:
1259:
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1252:
1250:
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1235:
1234:
1229:
1228:
1225:
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1220:
1217:
1215:
1212:
1210:
1206:
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1200:
1197:
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1191:
1190:
1189:
1185:
1183:
1179:
1176:
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1170:
1167:
1165:
1162:
1160:
1157:
1155:
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1150:
1147:
1145:
1142:
1141:
1140:
1139:
1134:
1131:
1130:
1127:
1124:
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1119:
1117:
1114:
1112:
1109:
1107:
1104:
1102:
1099:
1096:
1092:
1089:
1085:
1082:
1080:
1077:
1075:
1072:
1071:
1070:
1066:
1063:
1062:
1060:
1056:
1050:
1047:
1045:
1042:
1038:
1035:
1033:
1030:
1028:
1025:
1024:
1023:
1022:
1018:
1016:
1015:
1011:
1008:
1004:
1003:
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995:
992:
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987:
986:
985:
984:
980:
979:
977:
973:
970:
968:
964:
961:
959:
953:
949:
945:
938:
933:
931:
926:
924:
919:
918:
915:
909:
908:
900:
896:
891:
886:
882:
878:
874:
867:
864:
852:
848:
842:
839:
834:
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820:
816:
812:
808:
801:
798:
787:
783:
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774:
763:
759:
753:
750:
745:
741:
736:
731:
727:
723:
719:
715:
711:
704:
701:
696:
692:
687:
682:
677:
672:
668:
664:
660:
653:
651:
647:
642:
638:
633:
628:
624:
620:
616:
612:
608:
601:
598:
586:
582:
581:"COL1A2 gene"
576:
573:
568:
566:9780123971654
562:
558:
554:
550:
543:
541:
537:
526:
522:
516:
513:
506:
502:
499:
497:
494:
492:
489:
487:
484:
483:
479:
477:
474:
473:
465:
463:
461:
457:
455:
451:
447:
443:
439:
437:
432:
426:
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422:
416:
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405:
396:
389:
387:
384:
375:
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371:
367:
363:
359:
355:
351:
347:
343:
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328:
324:
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316:
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301:
297:
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274:
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267:
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261:
256:
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214:
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208:
205:
202:
200:
196:
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184:
180:
175:
170:
159:
156:
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146:
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137:
133:
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125:
122:
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116:
111:
108:
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99:
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84:
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75:
72:
69:
67:
63:
60:
57:
55:
51:
47:
43:
38:
33:
27:
19:
1490:Tropoelastin
1446:
1419:
1387:
1297:
1287:
1270:
1260:
1231:
1186:
1136:
1090:
1068:
1019:
1012:
1000:
981:
883:(1): 82–88.
880:
876:
866:
855:. Retrieved
850:
841:
814:
810:
800:
789:. Retrieved
785:
776:
765:. Retrieved
761:
752:
717:
713:
703:
669:(16): 2642.
666:
662:
614:
610:
600:
589:. Retrieved
584:
575:
548:
528:. Retrieved
524:
515:
475:
469:
458:
448:
444:
440:
433:
430:
417:
401:
379:
339:
331:
326:
323:eosinophilic
314:
313:
271:
190:Alt. symbols
126:
26:
1568:Cytokeratin
1497:Vitronectin
1178:multiplexin
344:as well as
342:scar tissue
293:Swiss-model
177:Identifiers
148:Swiss-model
40:Identifiers
1608:Categories
1199:Endostatin
1188:type XVIII
857:2023-09-27
791:2023-09-27
767:2023-09-27
591:2023-10-25
530:2023-10-25
507:References
421:nanometers
358:myofibrils
354:endomysium
289:Structures
284:Search for
273:q21.3-22.1
258:Other data
144:Structures
139:Search for
113:Other data
1624:Collagens
1578:Reticulin
1271:type VIII
551:: 71–84.
390:Structure
376:Formation
350:ligaments
240:NM_000089
199:NCBI gene
128:q21.3-q22
95:NM_000088
54:NCBI gene
1593:diseases
1589:See also
1532:Tectorin
1351:Leprecan
1261:type VII
1091:type XII
1014:type III
967:Collagen
899:26787413
833:12362985
744:33835418
695:34451183
663:Polymers
641:21967573
480:See also
319:collagen
303:InterPro
158:InterPro
1573:Gelatin
1564:Keratin
1512:Decorin
1485:Elastin
1380:Laminin
1356:ADAMTS2
1330:Enzymes
1320:COL28A1
1315:COL27A1
1308:COL11A2
1303:COL11A1
1298:type XI
1292:COL10A1
1233:type VI
1230:other:
1224:COL25A1
1219:COL23A1
1214:COL17A1
1209:COL13A1
1194:COL18A1
1182:COL15A1
1138:type IV
1126:COL22A1
1121:COL21A1
1116:COL20A1
1111:COL19A1
1106:COL16A1
1101:COL14A1
1095:COL12A1
1069:type IX
1049:COL26A1
1044:COL24A1
1002:type II
944:Protein
735:8403095
686:8399689
632:3430002
413:proline
346:tendons
335:Glycine
299:Domains
247:UniProt
154:Domains
124:Chr. 17
102:UniProt
1517:FAM20C
1288:type X
1281:COL8A2
1276:COL8A1
1265:COL7A1
1254:COL6A5
1249:COL6A3
1244:COL6A2
1239:COL6A1
1169:COL4A6
1164:COL4A5
1159:COL4A4
1154:COL4A3
1149:COL4A2
1144:COL4A1
1084:COL9A3
1079:COL9A2
1074:COL9A1
1037:COL5A3
1032:COL5A2
1027:COL5A1
1021:type V
1007:COL2A1
994:COL1A2
989:COL1A1
983:type I
958:matrix
897:
831:
742:
732:
693:
683:
639:
629:
563:
370:dentin
368:, the
366:dermis
364:, the
352:, the
269:Chr. 7
252:P08123
235:RefSeq
228:120160
185:COL1A2
182:Symbol
107:P02452
90:RefSeq
83:120150
48:COL1A1
45:Symbol
1557:Other
1542:TECTB
1537:TECTA
1507:FREM2
1502:FRAS1
1480:ALCAM
1473:Other
1462:LAMC3
1457:LAMC2
1452:LAMC1
1447:gamma
1440:LAMB4
1435:LAMB3
1430:LAMB2
1425:LAMB1
1413:LAMA5
1408:LAMA4
1403:LAMA3
1398:LAMA2
1393:LAMA1
1388:alpha
1065:FACIT
1058:Other
264:Locus
119:Locus
1522:ECM1
1420:beta
895:PMID
829:PMID
740:PMID
691:PMID
637:PMID
561:ISBN
470:See
411:and
362:bone
223:OMIM
216:2198
211:HGNC
204:1278
78:OMIM
71:2197
66:HGNC
59:1277
885:doi
881:173
819:doi
730:PMC
722:doi
681:PMC
671:doi
627:PMC
619:doi
615:441
553:doi
356:of
193:OI4
1610::
1180::
1135::
1067::
946::
893:.
879:.
875:.
849:.
827:.
815:49
813:.
809:.
784:.
760:.
738:.
728:.
718:12
716:.
712:.
689:.
679:.
667:13
665:.
661:.
649:^
635:.
625:.
613:.
609:.
583:.
559:.
539:^
523:.
456:.
348:,
1566:/
1349:/
1340:/
1294:)
1290:(
1267:)
1263:(
1097:)
1093:(
1009:)
1005:(
936:e
929:t
922:v
901:.
887::
860:.
835:.
821::
794:.
770:.
746:.
724::
697:.
673::
643:.
621::
594:.
569:.
555::
533:.
20:)
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