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http://purl.uniprot.org/citations/12668765http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12668765http://www.w3.org/2000/01/rdf-schema#comment"The Golgi-associated, gamma-adaptin homologous, ADP-ribosylation factor (ARF)-interacting proteins (GGAs) are adaptors that sort receptors from the trans-Golgi network into the endosomallysosomal pathway. The GGAs and TOM1 (GAT) domains of the GGAs are responsible for their ARF-dependent localization. The 2.4-A crystal structure of the GAT domain of human GGA1 reveals a three-helix bundle, with a long N-terminal helical extension that is not conserved in GAT domains that do not bind ARF. The ARF binding site is located in the N-terminal extension and is separate from the core three-helix bundle. An unanticipated structural similarity to the N-terminal domain of syntaxin 1a was discovered, comprising the entire three-helix bundle. A conserved binding site on helices 2 and 3 of the GAT domain three-helix bundle is predicted to interact with coiled-coil-containing proteins. We propose that the GAT domain is descended from the same ancestor as the syntaxin 1a N-terminal domain, and that both protein families share a common function in binding coiled-coil domain proteins."xsd:string
http://purl.uniprot.org/citations/12668765http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0831133100"xsd:string
http://purl.uniprot.org/citations/12668765http://purl.uniprot.org/core/author"Misra S."xsd:string
http://purl.uniprot.org/citations/12668765http://purl.uniprot.org/core/author"Hurley J.H."xsd:string
http://purl.uniprot.org/citations/12668765http://purl.uniprot.org/core/author"Suer S."xsd:string
http://purl.uniprot.org/citations/12668765http://purl.uniprot.org/core/author"Saidi L.F."xsd:string
http://purl.uniprot.org/citations/12668765http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12668765http://purl.uniprot.org/core/name"Proc Natl Acad Sci U S A"xsd:string
http://purl.uniprot.org/citations/12668765http://purl.uniprot.org/core/pages"4451-4456"xsd:string
http://purl.uniprot.org/citations/12668765http://purl.uniprot.org/core/title"Structure of the GAT domain of human GGA1: a syntaxin amino-terminal domain fold in an endosomal trafficking adaptor."xsd:string
http://purl.uniprot.org/citations/12668765http://purl.uniprot.org/core/volume"100"xsd:string
http://purl.uniprot.org/citations/12668765http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12668765
http://purl.uniprot.org/citations/12668765http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12668765
http://purl.uniprot.org/uniprot/P84077#attribution-E983FBF763FEC862D3F77E0D3C9C7DEAhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/12668765
http://purl.uniprot.org/uniprot/Q9UJY5#attribution-4E02E018C7CB5F8A9374E677CD43B853http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/12668765
http://purl.uniprot.org/uniprot/Q9UJY5#attribution-E983FBF763FEC862D3F77E0D3C9C7DEAhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/12668765
http://purl.uniprot.org/uniprot/#_Q9UJY5-mappedCitation-12668765http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12668765
http://purl.uniprot.org/uniprot/Q9UJY5http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12668765