1e42: Difference between revisions
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Revision as of 16:59, 5 November 2007
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BETA2-ADAPTIN APPENDAGE DOMAIN, FROM CLATHRIN ADAPTOR AP2
OverviewOverview
The heterotetrameric AP2 adaptor (alpha, beta 2, mu 2 and sigma 2, subunits) plays a central role in clathrin-mediated endocytosis. We, present the protein recruitment function and 1.7 A resolution structure of, its beta 2-appendage domain to complement those previously determined for, the mu 2 subunit and alpha appendage. Using structure-directed, mutagenesis, we demonstrate the ability of the beta 2 appendage alone to, bind directly to clathrin and the accessory proteins AP180, epsin and, eps15 at the same site. Clathrin polymerization is promoted by binding of, clathrin simultaneously to the beta 2-appendage site and to a second site, on the adjacent beta 2 hinge. This results in the displacement of the, other ligands from the beta 2 appendage. Thus clathrin binding to an, AP2-accessory protein complex would cause the controlled release of, accessory proteins at sites of vesicle formation.
About this StructureAbout this Structure
1E42 is a Single protein structure of sequence from Homo sapiens with CL, MG, NI, DTD and GOL as ligands. Structure known Active Sites: AC1, AC2, AC3, AC4 and AC5. Full crystallographic information is available from OCA.
ReferenceReference
The structure and function of the beta 2-adaptin appendage domain., Owen DJ, Vallis Y, Pearse BM, McMahon HT, Evans PR, EMBO J. 2000 Aug 15;19(16):4216-27. PMID:10944104
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