1e42: Difference between revisions

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[[Image:1e42.gif|left|200px]]
{{Seed}}
[[Image:1e42.png|left|200px]]


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{{STRUCTURE_1e42|  PDB=1e42  |  SCENE=  }}  
{{STRUCTURE_1e42|  PDB=1e42  |  SCENE=  }}  


'''BETA2-ADAPTIN APPENDAGE DOMAIN, FROM CLATHRIN ADAPTOR AP2'''
===BETA2-ADAPTIN APPENDAGE DOMAIN, FROM CLATHRIN ADAPTOR AP2===




==Overview==
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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.
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{{ABSTRACT_PUBMED_10944104}}


==About this Structure==
==About this Structure==
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[[Category: Adaptor]]
[[Category: Adaptor]]
[[Category: Endocytosis]]
[[Category: Endocytosis]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:38:15 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:07:04 2008''

Revision as of 21:07, 30 June 2008

File:1e42.png

Template:STRUCTURE 1e42

BETA2-ADAPTIN APPENDAGE DOMAIN, FROM CLATHRIN ADAPTOR AP2

Template:ABSTRACT PUBMED 10944104

About this Structure

1E42 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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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