1qts
CRYSTAL STRUCTURE OF THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE
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OverviewOverview
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 StructureAbout this Structure
1QTS is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
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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