24:
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This domain is approximately 150 amino acids in length and is always found located at the N-termini of proteins. The domain forms a compact globular structure, composed of nine alpha-helices connected by loops of varying length. The general topology is determined by three helical hairpins that are
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content. Epsin binding to membranes facilitates their deformation by insertion of the N-terminal helix into the inner leaflet of the bilayer, pushing the head groups apart. This would reduce the energy needed to curve the membrane into a vesicle, making it easier for the clathrin cage to fix and
228:
stacked consecutively with a right hand twist. An N-terminal helix folds back, forming a deep basic groove that forms the binding pocket for the Ins(1,4,5)P3 ligand. The lipid ligand is coordinated by residues from surrounding alpha-helices and all three phosphates are multiply coordinated.
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is able to recruit and promote clathrin polymerisation on a lipid monolayer, but may have additional roles in signalling and actin regulation. Epsin causes a strong degree of membrane curvature and tubulation, even fragmentation of membranes with a high
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stabilise the curved membrane. This points to a pioneering role for epsin in vesicle budding, as it provides both a driving force and a link between membrane invagination and clathrin polymerisation.
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115:
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suggesting that the domain is a membrane-interacting module. The main function of proteins containing this domain appears to be to act as accessory
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83:
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The N-terminal alpha-helix of this domain is hydrophobic and inserts into the membrane like a wedge and helps to drive membrane curvature.
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730:
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653:
191:
608:
531:
467:
797:
127:
480:
Ford MG, Mills IG, Peter BJ, et al. (September 2002). "Curvature of clathrin-coated pits driven by epsin".
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Ford MG, Mills IG, Peter BJ, et al. (September 2002). "Curvature of clathrin-coated pits driven by epsin".
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417:"Identification of a novel domain shared by putative components of the endocytic and cytoskeletal machinery"
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265:, however not all ENTH domains bind to this molecule. Binding causes tubulation of
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In particular, epsin-1 shows specificity for the membrane glycophospholipid
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Chen H, Bateman A, de
Camilli P, Hyman J, Panepucci E, Brunger AT (2002).
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this membrane-binding function is normally coordinated with
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Proteins containing this domain have been found to bind
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415:Kay BK, Yamabhai M, Wendland B, Emr SD (1999).
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205:epsin N-terminal homology (ENTH) domain
211:that is found in proteins involved in
18:
284:Human proteins containing this domain
263:phosphatidylinositol-4,5-bisphosphate
7:
232:Interactions with the lipid bilayer
14:
468:Endocytosis.org entry on epsin
1:
385:10.1016/S0014-5793(01)03306-3
143:Available protein structures:
869:Peripheral membrane proteins
885:
554:
248:adaptors in endocytosis,
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21:
28:ENTH domain of epsin-1.
494:10.1038/nature01020
337:10.1038/nature01020
433:10.1110/ps.8.2.435
851:
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368:"The ENTH domain"
209:structural domain
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192:structure summary
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277:polymerisation.
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864:Protein domains
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548:Protein domains
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488:(6905): 361–6.
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474:Further reading
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331:(6905): 361–6.
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104:OPM superfamily
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17:
16:InterPro Domain
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427:(2): 435–8.
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378:(1): 11–18.
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242:Ins(1,4,5)P3
235:
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217:cytoskeletal
204:
202:
843:zinc finger
421:Protein Sci
219:machinery.
213:endocytosis
116:OPM protein
34:Identifiers
858:Categories
307:References
155:structures
731:EcoEI_R_C
372:FEBS Lett
267:liposomes
223:Structure
77:PDOC50942
65:IPR001026
502:12353027
451:10048338
402:25544319
394:11911874
345:12353027
275:clathrin
246:clathrin
172:RCSB PDB
60:InterPro
761:Kringle
654:CGI-121
624:BTB/POZ
510:4372368
442:2144257
353:4372368
299:;
271:in vivo
133:cd03571
72:PROSITE
53:PF01417
508:
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482:Nature
449:
439:
400:
392:
351:
343:
325:Nature
293:ENTHD1
289:CLINT1
187:PDBsum
161:
151:
97:SUPFAM
39:Symbol
776:NACHT
699:Pyrin
679:Death
644:Cache
579:ADF-H
506:S2CID
398:S2CID
349:S2CID
295:;
291:;
250:epsin
207:is a
93:SCOPe
84:SCOP2
828:WD40
823:TRIO
756:HEAT
751:FYVE
746:FGGY
741:ENTH
721:DHR2
716:DHR1
711:DHHC
694:CARD
674:CVHN
629:BZIP
604:BESS
589:ARID
584:ANTH
569:ACDC
498:PMID
447:PMID
390:PMID
341:PMID
301:EPN3
297:EPN2
269:and
240:and
215:and
203:The
180:PDBj
176:PDBe
159:ECOD
149:Pfam
121:1h0a
89:1edu
48:Pfam
42:ENTH
838:YTH
818:SUN
813:SH3
808:SH2
793:PDZ
786:LOV
781:PAS
771:LRR
766:LIM
736:EF1
706:DEP
689:DED
669:CUT
664:CUB
659:CRM
649:CBS
619:BPS
614:BMC
609:BIR
599:BEN
594:BAR
574:ACT
564:ABM
490:doi
486:419
437:PMC
429:doi
380:doi
376:513
333:doi
329:419
167:PDB
128:CDD
860::
833:X8
803:PX
798:PH
726:DM
684:DD
639:C2
634:C1
559:3H
504:.
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315:^
303:;
178:;
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109:38
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540:e
533:t
526:v
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425:8
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335::
Text is available under the Creative Commons Attribution-ShareAlike License. Additional terms may apply.
