31:
1082:
Dunker, A. K.; Lawson, J. D.; Brown, C. J.; Williams, R. M.; Romero, P; Oh, J. S.; Oldfield, C. J.; Campen, A. M.; Ratliff, C. M.; Hipps, K. W.; Ausio, J; Nissen, M. S.; Reeves, R; Kang, C; Kissinger, C. R.; Bailey, R. W.; Griswold, M. D.; Chiu, W; Garner, E. C.; Obradovic, Z (2001). "Intrinsically
448:). Rational protein design approaches make protein-sequence predictions that will fold to specific structures. These predicted sequences can then be validated experimentally through methods such as
514:
30:
79:
785:
Greene, Lesley H.; Lewis, Tony E.; Addou, Sarah; Cuff, Alison; Dallman, Tim; Dibley, Mark; Redfern, Oliver; Pearl, Frances; Nambudiry, Rekha (2007-01-01).
486:
507:
286:
either by inserting into it, or being tethered via a covalently attached lipid. They are one of the common types of protein along with soluble
474:
1039:; Sonnhammer, E. L. L. (2001). "Predicting transmembrane protein topology with a hidden markov model: Application to complete genomes".
787:"The CATH domain structure database: new protocols and classification levels give a more comprehensive resource for exploring evolution"
500:
314:
844:"SCOPe: Structural Classification of Proteins—extended, integrating SCOP and ASTRAL data and classification of new structures"
329:, and large multi-domain proteins connected by flexible linkers. They constitute one of the main types of protein (alongside
1174:
Dunker AK, Silman I, Uversky VN, Sussman JL (December 2008). "Function and structure of inherently disordered proteins".
523:
318:
47:
457:
453:
78:
Four large classes of protein that are generally agreed upon by the two main structure classification databases (
55:
421:
1215:
1092:
263:
599:
417:
413:
409:
358:
165:
157:
63:
354:
283:
1097:
635:
469:
444:
design) or by making calculated variations on a known protein structure and its sequence (known as
232:
181:
161:
138:
99:
59:
1156:
1064:
1014:
405:
298:. They are targets of over 50% of all modern medicinal drugs. It is estimated that 20–30% of all
295:
1191:
1148:
1110:
1056:
1036:
1006:
989:
Overington JP, Al-Lazikani B, Hopkins AL (December 2006). "How many drug targets are there?".
971:
919:
881:
863:
824:
806:
767:
749:
655:
547:
449:
378:
321:. IDPs cover a spectrum of states from fully unstructured to partially structured and include
287:
228:
177:
134:
95:
67:
39:
1183:
1140:
1102:
1048:
998:
961:
953:
911:
871:
855:
814:
798:
757:
741:
650:
573:
338:
330:
279:
193:
902:
Efimov, Alexander V. (1995). "Structural
Similarity between Two-layer α/β and β-Proteins".
676:
640:
542:
334:
255:
208:
728:
Hubbard, Tim J. P.; Murzin, Alexey G.; Brenner, Steven E.; Chothia, Cyrus (1997-01-01).
966:
941:
876:
843:
819:
786:
681:
609:
578:
537:
437:
326:
212:
1106:
762:
729:
1209:
1131:, Wright PE (March 2005). "Intrinsically unstructured proteins and their functions".
645:
401:
350:
291:
83:
1160:
1068:
1018:
1032:
563:
390:
34:
A summary of functional annotation of the most ancestral translation protein folds
604:
568:
322:
236:
185:
146:
118:
114:
103:
1187:
1128:
686:
630:
614:
583:
259:
244:
240:
216:
197:
189:
153:
142:
107:
17:
867:
810:
753:
492:
702:
671:
1195:
1152:
1114:
1060:
1052:
1010:
975:
915:
885:
828:
745:
957:
923:
859:
771:
802:
366:
122:
374:
370:
362:
51:
842:
Fox, Naomi K.; Brenner, Steven E.; Chandonia, John-Marc (2014-01-01).
382:
377:. The roles of such proteins include protection and support, forming
303:
1144:
1002:
440:
and do not exist in nature. Proteins can be designed from scratch (
29:
480:
425:
386:
299:
496:
942:"SCOP2 prototype: a new approach to protein structure mining"
404:
typically have a tertiary structure that is maintained by
730:"SCOP: a Structural Classification of Proteins database"
62:
proportions. Each class contains multiple, independent
695:
664:
623:
592:
556:
530:
935:
933:
897:
895:
145:, with the possible exception of a few isolated
106:, with the possible exception of a few isolated
262:and leucine-rich-repeat (LRR) proteins such as
436:Numerous protein structures are the result of
1085:Journal of Molecular Graphics & Modelling
508:
8:
515:
501:
493:
349:Coiled coil proteins form long, insoluble
1096:
965:
875:
818:
761:
27:Categories of protein tertiary structure
720:
7:
50:topology. They describe groups of
25:
315:Intrinsically disordered proteins
310:Intrinsically disordered proteins
192:that occur separately along the
548:Structure determination methods
357:. There are many scleroprotein
133:All-β proteins are a class of
94:All-α proteins are a class of
1:
1107:10.1016/s1093-3263(00)00138-8
1041:Journal of Molecular Biology
904:Journal of Molecular Biology
254:Common examples include the
227:α/β proteins are a class of
207:Common examples include the
176:α+β proteins are a class of
152:Common examples include the
113:Common examples include the
74:Generally recognised classes
319:three-dimensional structure
235:is composed of alternating
1232:
952:(Database issue): D310–4.
524:Protein tertiary structure
306:encode membrane proteins.
66:(i.e. are not necessarily
48:protein tertiary structure
1188:10.1016/j.sbi.2008.10.002
458:Artificial gene synthesis
454:site-directed mutagenesis
243:along the backbone. The
1176:Curr. Opin. Struct. Biol
1133:Nat. Rev. Mol. Cell Biol
317:lack a fixed or ordered
141:is composed entirely of
102:is composed entirely of
46:are broad categories of
1053:10.1006/jmbi.2000.4315
916:10.1006/jmbi.1994.0033
848:Nucleic Acids Research
797:(suppl 1): D291–D297.
791:Nucleic Acids Research
734:Nucleic Acids Research
418:metal-binding proteins
410:cysteine-rich proteins
264:ribonuclease inhibitor
68:evolutionarily related
35:
1083:disordered protein".
600:Immunoglobulin domain
247:are therefore mostly
200:are therefore mostly
166:B3 DNA binding domain
158:beta-propeller domain
64:protein superfamilies
33:
940:Andreeva, A (2014).
746:10.1093/nar/25.1.236
355:extracellular matrix
345:Coiled coil proteins
284:biological membranes
44:protein fold classes
991:Nat Rev Drug Discov
958:10.1093/nar/gkt1242
860:10.1093/nar/gkt1240
636:Leucine-rich repeat
470:Protein superfamily
296:disordered proteins
233:secondary structure
182:secondary structure
162:immunoglobulin fold
139:secondary structure
100:secondary structure
60:secondary structure
54:that share similar
1035:; Larsson, B. R.;
803:10.1093/nar/gkl959
406:disulphide bridges
270:Additional classes
229:structural domains
178:structural domains
149:on the periphery.
135:structural domains
110:on the periphery.
96:structural domains
36:
946:Nucleic Acids Res
854:(D1): D304–D309.
711:
710:
656:Trefoil knot fold
538:Structural domain
450:peptide synthesis
432:Designed proteins
379:connective tissue
339:membrane proteins
288:globular proteins
280:Membrane proteins
275:Membrane proteins
70:to one another).
40:molecular biology
16:(Redirected from
1223:
1200:
1199:
1171:
1165:
1164:
1125:
1119:
1118:
1100:
1079:
1073:
1072:
1029:
1023:
1022:
986:
980:
979:
969:
937:
928:
927:
899:
890:
889:
879:
839:
833:
832:
822:
782:
776:
775:
765:
725:
696:Irregular folds:
651:Thioredoxin fold
574:Homeodomain fold
517:
510:
503:
494:
446:protein redesign
353:involved in the
292:fibrous proteins
21:
1231:
1230:
1226:
1225:
1224:
1222:
1221:
1220:
1206:
1205:
1204:
1203:
1173:
1172:
1168:
1145:10.1038/nrm1589
1127:
1126:
1122:
1081:
1080:
1076:
1031:
1030:
1026:
1003:10.1038/nrd2199
988:
987:
983:
939:
938:
931:
901:
900:
893:
841:
840:
836:
784:
783:
779:
727:
726:
722:
717:
712:
707:
691:
677:Ferredoxin fold
660:
641:Flavodoxin fold
619:
588:
552:
543:Protein folding
526:
521:
466:
438:rational design
434:
399:
347:
327:molten globules
312:
277:
272:
256:flavodoxin fold
225:
209:ferredoxin fold
184:is composed of
174:
131:
92:
76:
28:
23:
22:
15:
12:
11:
5:
1229:
1227:
1219:
1218:
1208:
1207:
1202:
1201:
1166:
1139:(3): 197–208.
1120:
1098:10.1.1.113.556
1074:
1047:(3): 567–580.
1037:Von Heijne, G.
1024:
981:
929:
910:(4): 402–415.
891:
834:
777:
740:(1): 236–239.
719:
718:
716:
713:
709:
708:
706:
705:
699:
697:
693:
692:
690:
689:
684:
682:Ribonuclease A
679:
674:
668:
666:
662:
661:
659:
658:
653:
648:
643:
638:
633:
627:
625:
621:
620:
618:
617:
612:
610:Beta-propeller
607:
602:
596:
594:
590:
589:
587:
586:
581:
579:Alpha solenoid
576:
571:
566:
560:
558:
554:
553:
551:
550:
545:
540:
534:
532:
528:
527:
522:
520:
519:
512:
505:
497:
491:
490:
484:
478:
472:
465:
462:
433:
430:
402:Small proteins
398:
397:Small proteins
395:
346:
343:
311:
308:
282:interact with
276:
273:
271:
268:
224:
221:
213:ribonuclease A
173:
170:
130:
127:
91:
88:
75:
72:
26:
24:
18:All-α proteins
14:
13:
10:
9:
6:
4:
3:
2:
1228:
1217:
1216:Protein folds
1214:
1213:
1211:
1197:
1193:
1189:
1185:
1182:(6): 756–64.
1181:
1177:
1170:
1167:
1162:
1158:
1154:
1150:
1146:
1142:
1138:
1134:
1130:
1124:
1121:
1116:
1112:
1108:
1104:
1099:
1094:
1090:
1086:
1078:
1075:
1070:
1066:
1062:
1058:
1054:
1050:
1046:
1042:
1038:
1034:
1028:
1025:
1020:
1016:
1012:
1008:
1004:
1000:
997:(12): 993–6.
996:
992:
985:
982:
977:
973:
968:
963:
959:
955:
951:
947:
943:
936:
934:
930:
925:
921:
917:
913:
909:
905:
898:
896:
892:
887:
883:
878:
873:
869:
865:
861:
857:
853:
849:
845:
838:
835:
830:
826:
821:
816:
812:
808:
804:
800:
796:
792:
788:
781:
778:
773:
769:
764:
759:
755:
751:
747:
743:
739:
735:
731:
724:
721:
714:
704:
701:
700:
698:
694:
688:
687:SH2-like fold
685:
683:
680:
678:
675:
673:
670:
669:
667:
663:
657:
654:
652:
649:
647:
646:Rossmann fold
644:
642:
639:
637:
634:
632:
629:
628:
626:
622:
616:
613:
611:
608:
606:
603:
601:
598:
597:
595:
591:
585:
582:
580:
577:
575:
572:
570:
567:
565:
562:
561:
559:
555:
549:
546:
544:
541:
539:
536:
535:
533:
529:
525:
518:
513:
511:
506:
504:
499:
498:
495:
488:
485:
482:
479:
476:
473:
471:
468:
467:
463:
461:
459:
455:
451:
447:
443:
439:
431:
429:
427:
423:
419:
415:
414:metal ligands
411:
407:
403:
396:
394:
392:
388:
387:bone matrices
384:
380:
376:
372:
368:
364:
360:
359:superfamilies
356:
352:
344:
342:
340:
336:
332:
328:
324:
320:
316:
309:
307:
305:
301:
297:
293:
289:
285:
281:
274:
269:
267:
265:
261:
257:
252:
250:
246:
242:
238:
234:
231:in which the
230:
222:
220:
218:
214:
210:
205:
203:
199:
195:
191:
187:
183:
180:in which the
179:
171:
169:
167:
163:
159:
155:
150:
148:
144:
140:
137:in which the
136:
128:
126:
124:
120:
116:
111:
109:
105:
101:
98:in which the
97:
89:
87:
85:
81:
73:
71:
69:
65:
61:
57:
53:
49:
45:
41:
32:
19:
1179:
1175:
1169:
1136:
1132:
1123:
1091:(1): 26–59.
1088:
1084:
1077:
1044:
1040:
1027:
994:
990:
984:
949:
945:
907:
903:
851:
847:
837:
794:
790:
780:
737:
733:
723:
593:All-β folds:
564:Helix bundle
557:All-α folds:
445:
441:
435:
400:
391:muscle fiber
348:
323:random coils
313:
278:
253:
248:
226:
206:
202:antiparallel
201:
175:
151:
132:
112:
93:
77:
43:
37:
605:Beta barrel
569:Globin fold
119:globin fold
115:bromodomain
715:References
665:α+β folds:
631:TIM barrel
624:α/β folds:
615:Beta helix
584:Death fold
420:), and or
361:including
260:TIM barrel
217:SH2 domain
215:, and the
154:SH3 domain
56:amino acid
1093:CiteSeerX
1033:Krogh, A.
868:0305-1048
811:0305-1048
754:0305-1048
703:Conotoxin
672:DNA clamp
422:cofactors
245:β-strands
241:β-strands
237:α-helices
198:β-strands
190:β-strands
186:α-helices
147:α-helices
104:α-helices
1210:Category
1196:18952168
1161:18068406
1153:15738986
1129:Dyson HJ
1115:11381529
1069:15769874
1061:11152613
1019:11979420
1011:17139284
976:24293656
886:24304899
829:17135200
489:database
483:database
477:database
464:See also
424:such as
367:collagen
331:globular
325:, (pre-)
302:in most
249:parallel
194:backbone
143:β-sheets
121:and the
108:β-sheets
52:proteins
967:3964979
924:7837272
877:3965108
820:1751535
772:9016544
531:General
442:de novo
383:tendons
375:fibroin
371:elastin
363:keratin
335:fibrous
304:genomes
1194:
1159:
1151:
1113:
1095:
1067:
1059:
1017:
1009:
974:
964:
922:
884:
874:
866:
827:
817:
809:
770:
763:146380
760:
752:
389:, and
373:, and
351:fibers
294:, and
258:, the
196:. The
160:, the
156:, the
129:all-β
117:, the
90:all-α
1157:S2CID
1065:S2CID
1015:S2CID
456:, or
300:genes
1192:PMID
1149:PMID
1111:PMID
1057:PMID
1007:PMID
972:PMID
920:PMID
882:PMID
864:ISSN
825:PMID
807:ISSN
768:PMID
750:ISSN
487:FSSP
481:CATH
475:SCOP
426:heme
337:and
239:and
223:α/β
188:and
172:α+β
164:and
84:CATH
82:and
80:SCOP
58:and
1184:doi
1141:doi
1103:doi
1049:doi
1045:305
999:doi
962:PMC
954:doi
912:doi
908:245
872:PMC
856:doi
815:PMC
799:doi
758:PMC
742:doi
412:),
341:).
86:).
38:In
1212::
1190:.
1180:18
1178:.
1155:.
1147:.
1135:.
1109:.
1101:.
1089:19
1087:.
1063:.
1055:.
1043:.
1013:.
1005:.
993:.
970:.
960:.
950:42
948:.
944:.
932:^
918:.
906:.
894:^
880:.
870:.
862:.
852:42
850:.
846:.
823:.
813:.
805:.
795:35
793:.
789:.
766:.
756:.
748:.
738:25
736:.
732:.
460:.
452:,
428:.
393:.
385:,
381:,
369:,
365:,
333:,
290:,
266:.
251:.
219:.
211:,
204:.
168:.
125:.
42:,
1198:.
1186::
1163:.
1143::
1137:6
1117:.
1105::
1071:.
1051::
1021:.
1001::
995:5
978:.
956::
926:.
914::
888:.
858::
831:.
801::
774:.
744::
516:e
509:t
502:v
416:(
408:(
123:s
20:)
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