1eyh
CRYSTAL STRUCTURE OF THE EPSIN N-TERMINAL HOMOLOGY (ENTH) DOMAIN AT 1.56 ANGSTROM RESOLUTIONCRYSTAL STRUCTURE OF THE EPSIN N-TERMINAL HOMOLOGY (ENTH) DOMAIN AT 1.56 ANGSTROM RESOLUTION
FunctionFunction
[EPN1_RAT] Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations. Regulates receptor-mediated endocytosis.[1] [2] [3]
About this StructureAbout this Structure
1eyh is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Chen H, Fre S, Slepnev VI, Capua MR, Takei K, Butler MH, Di Fiore PP, De Camilli P. Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis. Nature. 1998 Aug 20;394(6695):793-7. PMID:9723620 doi:http://dx.doi.org/10.1038/29555
- ↑ Itoh T, Koshiba S, Kigawa T, Kikuchi A, Yokoyama S, Takenawa T. Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis. Science. 2001 Feb 9;291(5506):1047-51. PMID:11161217 doi:http://dx.doi.org/10.1126/science.291.5506.1047
- ↑ Ford MG, Mills IG, Peter BJ, Vallis Y, Praefcke GJ, Evans PR, McMahon HT. Curvature of clathrin-coated pits driven by epsin. Nature. 2002 Sep 26;419(6905):361-6. PMID:12353027 doi:10.1038/nature01020