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http://purl.uniprot.org/citations/10430869http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10430869http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10430869http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/10430869http://purl.org/dc/terms/identifier"doi:10.1073/pnas.96.16.8907"xsd:string
http://purl.uniprot.org/citations/10430869http://purl.org/dc/terms/identifier"doi:10.1073/pnas.96.16.8907"xsd:string
http://purl.uniprot.org/citations/10430869http://purl.uniprot.org/core/author"Fremont D.H."xsd:string
http://purl.uniprot.org/citations/10430869http://purl.uniprot.org/core/author"Fremont D.H."xsd:string
http://purl.uniprot.org/citations/10430869http://purl.uniprot.org/core/author"Traub L.M."xsd:string
http://purl.uniprot.org/citations/10430869http://purl.uniprot.org/core/author"Traub L.M."xsd:string
http://purl.uniprot.org/citations/10430869http://purl.uniprot.org/core/author"Downs M.A."xsd:string
http://purl.uniprot.org/citations/10430869http://purl.uniprot.org/core/author"Downs M.A."xsd:string
http://purl.uniprot.org/citations/10430869http://purl.uniprot.org/core/author"Westrich J.L."xsd:string
http://purl.uniprot.org/citations/10430869http://purl.uniprot.org/core/author"Westrich J.L."xsd:string
http://purl.uniprot.org/citations/10430869http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10430869http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10430869http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/10430869http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/10430869http://purl.uniprot.org/core/pages"8907-8912"xsd:string
http://purl.uniprot.org/citations/10430869http://purl.uniprot.org/core/pages"8907-8912"xsd:string
http://purl.uniprot.org/citations/10430869http://purl.uniprot.org/core/title"Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly."xsd:string
http://purl.uniprot.org/citations/10430869http://purl.uniprot.org/core/title"Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly."xsd:string
http://purl.uniprot.org/citations/10430869http://purl.uniprot.org/core/volume"96"xsd:string
http://purl.uniprot.org/citations/10430869http://purl.uniprot.org/core/volume"96"xsd:string
http://purl.uniprot.org/citations/10430869http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10430869
http://purl.uniprot.org/citations/10430869http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10430869