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1qts
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1qtp|1QTP]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qts OCA], [http://www.ebi.ac.uk/pdbsum/1qts PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qts RCSB]</span> | ||
}} | }} | ||
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[[Category: selenomethionine]] | [[Category: selenomethionine]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:18:54 2008'' |
Revision as of 20:18, 30 March 2008
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| , resolution 1.40Å | |||||||
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| Related: | 1QTP
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
1QTS 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
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