1qtp
From Proteopedia
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'''CRYSTAL STRUCTURE OF THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE''' | '''CRYSTAL STRUCTURE OF THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE''' | ||
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[[Category: Traub, L M.]] | [[Category: Traub, L M.]] | ||
[[Category: Westrich, J L.]] | [[Category: Westrich, J L.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:41:34 2008'' | |
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Revision as of 03:41, 3 May 2008
CRYSTAL STRUCTURE OF THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE
Overview
AP-2 adaptors regulate clathrin-bud formation at the cell surface by recruiting clathrin trimers to the plasma membrane and by selecting certain membrane proteins for inclusion within the developing clathrin-coat structure. These functions are performed by discrete subunits of the adaptor heterotetramer. The carboxyl-terminal appendage of the AP-2 alpha subunit appears to regulate the translocation of several endocytic accessory proteins to the bud site. We have determined the crystal structure of the alpha appendage at 1.4-A resolution by multiwavelength anomalous diffraction phasing. It is composed of two distinct structural modules, a beta-sandwich domain and a mixed alpha-beta platform domain. Structure-based mutagenesis shows that alterations to the molecular surface of a highly conserved region on the platform domain differentially affect associations of the appendage with amphiphysin, eps15, epsin, and AP180, revealing a common protein-binding interface.
About this Structure
1QTP is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly., Traub LM, Downs MA, Westrich JL, Fremont DH, Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8907-12. PMID:10430869 Page seeded by OCA on Sat May 3 06:41:34 2008
