29:
363:
Marsden I, Jin C, Liao X (May 1998). "Structural changes in the region directly adjacent to the DNA-binding helix highlight a possible mechanism to explain the observed changes in the sequence-specific binding of winged helix proteins".
335:. Members of the class O of forkhead box transcription factors (FoxO) have important roles in metabolism, cellular proliferation, stress tolerance and probably lifespan.
331:. Although the domain is found in several different transcription factors, a common function is their involvement in early developmental decisions of cell fates during
164:
76:
100:
495:
Clark KL, Halay ED, Lai E, Burley SK (July 1993). "Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5".
320:
184:
453:"The homeotic gene fork head encodes a nuclear protein and is expressed in the terminal regions of the Drosophila embryo"
301:, containing around 100 amino acids, which has since been identified in a number of transcription factors (including
306:
120:
654:
315:
172:
285:
592:
van der Horst A, Burgering BM (June 2007). "Stressing the role of FoxO proteins in lifespan and disease".
81:
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268:
113:
289:, a transcription factor that promotes terminal rather than segmental development, contains neither
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characteristic of other transcription factors. Instead, it contains a distinct type of
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332:
105:
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HCM1, etc.). This is referred to as the fork head domain but is also known as a "
69:
543:"Developmentally regulated Drosophila gene family encoding the fork head domain"
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as a monomer, but shows no similarity to previously identified DNA-binding
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28:
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Häcker U, Grossniklaus U, Gehring WJ, Jäckle H (September 1992).
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Weigel D, Jürgens G, Küttner F, Seifert E, Jäckle H (May 1989).
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52:
272:
16:
DNA-binding protein domain found in transcription factors
631:
This article incorporates text from the public domain
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33:Structure of the winged helix protein Genesis.
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8:
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27:
568:
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468:
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355:
401:"Five years on the wings of fork head"
18:
594:Nature Reviews Molecular Cell Biology
7:
399:Kaufmann E, Knöchel W (June 1996).
14:
323:". The fork head domain binds
1:
271:and whose purpose is to bind
136:Available protein structures:
547:Proc. Natl. Acad. Sci. U.S.A
470:10.1016/0092-8674(89)90133-5
418:10.1016/0925-4773(96)00539-4
671:
630:
283:The fork head protein of
131:
26:
316:Saccharomyces cerevisiae
560:10.1073/pnas.89.18.8754
286:Drosophila melanogaster
267:that is often found in
378:10.1006/jmbi.1998.1703
269:transcription factors
299:DNA-binding region
305:FD1-5, mammalian
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185:structure summary
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509:10.1038/364412a0
503:(6436): 412–20.
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261:fork head domain
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133:
31:
22:Fork head domain
19:
670:
669:
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655:Protein domains
645:
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606:10.1038/nrm2190
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303:D. melanogaster
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34:
17:
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5:
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584:
553:(18): 8754–8.
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265:protein domain
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2:
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600:(6): 440–50.
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463:(4): 645–58.
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333:embryogenesis
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263:is a type of
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460:
456:
408:
404:
394:
372:(2): 293–9.
369:
366:J. Mol. Biol
365:
358:
345:FOX proteins
321:winged helix
314:
302:
295:zinc-fingers
291:homeodomains
284:
282:
260:
258:
411:(1): 3–20.
39:Identifiers
351:References
148:structures
641:IPR001766
405:Mech. Dev
243:,
237:,
231:,
225:,
219:,
213:,
207:,
201:,
94:PDOC00564
70:IPR001766
47:Fork_head
649:Category
637:InterPro
622:31546098
614:17522590
435:18056224
339:See also
309:, human
279:Function
165:RCSB PDB
65:InterPro
579:1356269
525:4363526
517:8332212
479:2566386
427:8817449
386:9571051
249:
126:cd00059
89:PROSITE
82:SM00339
58:PF00250
620:
612:
577:
567:
523:
515:
497:Nature
477:
433:
425:
384:
329:motifs
180:PDBsum
154:
144:
114:SUPFAM
44:Symbol
618:S2CID
570:49999
521:S2CID
431:S2CID
325:B-DNA
110:SCOPe
101:SCOP2
77:SMART
635:and
633:Pfam
610:PMID
575:PMID
513:PMID
475:PMID
457:Cell
423:PMID
382:PMID
311:HTLF
307:HNF3
293:nor
259:The
246:2hfh
240:2hdc
234:2d2w
228:2c6y
222:2a3s
216:1kq8
210:1jxs
204:1e17
198:1d5v
173:PDBj
169:PDBe
152:ECOD
142:Pfam
106:2hfh
53:Pfam
602:doi
565:PMC
555:doi
505:doi
501:364
465:doi
413:doi
374:doi
370:278
273:DNA
192:PDB
160:PDB
121:CDD
651::
639::
616:.
608:.
596:.
573:.
563:.
551:89
549:.
545:.
533:^
519:.
511:.
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487:^
473:.
461:57
459:.
455:.
443:^
429:.
421:.
409:57
407:.
403:.
380:.
368:.
313:,
275:.
171:;
167:;
150:/
112:/
108:/
624:.
604::
598:8
581:.
557::
527:.
507::
481:.
467::
437:.
415::
388:.
376::
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