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| [[Image:1qts.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1qts| PDB=1qts | SCENE= }} | | {{STRUCTURE_1qts| PDB=1qts | SCENE= }} |
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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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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_10430869}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10430869 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10430869}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Membrane protein]] | | [[Category: Membrane protein]] |
| [[Category: Selenomethionine]] | | [[Category: Selenomethionine]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:41:48 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:03:47 2008'' |