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http://purl.uniprot.org/citations/16155582http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16155582http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16155582http://www.w3.org/2000/01/rdf-schema#comment"Sec15, a component of the exocyst, recognizes vesicle-associated Rab GTPases, helps target transport vesicles to the budding sites in yeast and is thought to recruit other exocyst proteins. Here we report the characterization of a 35-kDa fragment that comprises most of the C-terminal half of Drosophila melanogaster Sec15. This C-terminal domain was found to bind a subset of Rab GTPases, especially Rab11, in a GTP-dependent manner. We also provide evidence that in fly photoreceptors Sec15 colocalizes with Rab11 and that loss of Sec15 affects rhabdomere morphology. Determination of the 2.5-A crystal structure of the C-terminal domain revealed a novel fold consisting of ten alpha-helices equally distributed between two subdomains (N and C subdomains). We show that the C subdomain, mainly via a single helix, is sufficient for Rab binding."xsd:string
http://purl.uniprot.org/citations/16155582http://purl.org/dc/terms/identifier"doi:10.1038/nsmb987"xsd:string
http://purl.uniprot.org/citations/16155582http://purl.org/dc/terms/identifier"doi:10.1038/nsmb987"xsd:string
http://purl.uniprot.org/citations/16155582http://purl.uniprot.org/core/author"Wu S."xsd:string
http://purl.uniprot.org/citations/16155582http://purl.uniprot.org/core/author"Wu S."xsd:string
http://purl.uniprot.org/citations/16155582http://purl.uniprot.org/core/author"Quiocho F.A."xsd:string
http://purl.uniprot.org/citations/16155582http://purl.uniprot.org/core/author"Quiocho F.A."xsd:string
http://purl.uniprot.org/citations/16155582http://purl.uniprot.org/core/author"Bellen H.J."xsd:string
http://purl.uniprot.org/citations/16155582http://purl.uniprot.org/core/author"Bellen H.J."xsd:string
http://purl.uniprot.org/citations/16155582http://purl.uniprot.org/core/author"Pichaud F."xsd:string
http://purl.uniprot.org/citations/16155582http://purl.uniprot.org/core/author"Pichaud F."xsd:string
http://purl.uniprot.org/citations/16155582http://purl.uniprot.org/core/author"Mehta S.Q."xsd:string
http://purl.uniprot.org/citations/16155582http://purl.uniprot.org/core/author"Mehta S.Q."xsd:string
http://purl.uniprot.org/citations/16155582http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16155582http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16155582http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/16155582http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/16155582http://purl.uniprot.org/core/pages"879-885"xsd:string
http://purl.uniprot.org/citations/16155582http://purl.uniprot.org/core/pages"879-885"xsd:string
http://purl.uniprot.org/citations/16155582http://purl.uniprot.org/core/title"Sec15 interacts with Rab11 via a novel domain and affects Rab11 localization in vivo."xsd:string
http://purl.uniprot.org/citations/16155582http://purl.uniprot.org/core/title"Sec15 interacts with Rab11 via a novel domain and affects Rab11 localization in vivo."xsd:string
http://purl.uniprot.org/citations/16155582http://purl.uniprot.org/core/volume"12"xsd:string
http://purl.uniprot.org/citations/16155582http://purl.uniprot.org/core/volume"12"xsd:string