1e42: Difference between revisions

Revision as of 13:23, 21 February 2008

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 , , , and as ligands. Known structural/functional Sites: , , , and . 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

Page seeded by OCA on Thu Feb 21 12:23:35 2008

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OCA

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 ==Overview==
-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.
+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 Structure==
@@ Line 13: / Line 13: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Evans, P.R.]]
+[[Category: Evans, P R.]]
-[[Category: Mcmahon, H.T.]]
+[[Category: Mcmahon, H T.]]
-[[Category: Owen, D.J.]]
+[[Category: Owen, D J.]]
 [[Category: CL]]
 [[Category: DTD]]
@@ Line 24: / Line 24: @@
 [[Category: endocytosis]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:37:03 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:23:35 2008''