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http://purl.uniprot.org/citations/10025402http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10025402http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10025402http://www.w3.org/2000/01/rdf-schema#comment"The small G protein Rab3A plays an important role in the regulation of neurotransmitter release. The crystal structure of activated Rab3A/GTP/Mg2+ bound to the effector domain of rabphilin-3A was solved to 2.6 A resolution. Rabphilin-3A contacts Rab3A in two distinct areas. The first interface involves the Rab3A switch I and switch II regions, which are sensitive to the nucleotide-binding state of Rab3A. The second interface consists of a deep pocket in Rab3A that interacts with a SGAWFF structural element of rabphilin-3A. Sequence and structure analysis, and biochemical data suggest that this pocket, or Rab complementarity-determining region (RabCDR), establishes a specific interaction between each Rab protein and its effectors. RabCDRs could be major determinants of effector specificity during vesicle trafficking and fusion."xsd:string
http://purl.uniprot.org/citations/10025402http://purl.org/dc/terms/identifier"doi:10.1016/s0092-8674(00)80549-8"xsd:string
http://purl.uniprot.org/citations/10025402http://purl.org/dc/terms/identifier"doi:10.1016/s0092-8674(00)80549-8"xsd:string
http://purl.uniprot.org/citations/10025402http://purl.uniprot.org/core/author"Brunger A.T."xsd:string
http://purl.uniprot.org/citations/10025402http://purl.uniprot.org/core/author"Brunger A.T."xsd:string
http://purl.uniprot.org/citations/10025402http://purl.uniprot.org/core/author"Ostermeier C."xsd:string
http://purl.uniprot.org/citations/10025402http://purl.uniprot.org/core/author"Ostermeier C."xsd:string
http://purl.uniprot.org/citations/10025402http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10025402http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10025402http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/10025402http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/10025402http://purl.uniprot.org/core/pages"363-374"xsd:string
http://purl.uniprot.org/citations/10025402http://purl.uniprot.org/core/pages"363-374"xsd:string
http://purl.uniprot.org/citations/10025402http://purl.uniprot.org/core/title"Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A."xsd:string
http://purl.uniprot.org/citations/10025402http://purl.uniprot.org/core/title"Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A."xsd:string
http://purl.uniprot.org/citations/10025402http://purl.uniprot.org/core/volume"96"xsd:string
http://purl.uniprot.org/citations/10025402http://purl.uniprot.org/core/volume"96"xsd:string
http://purl.uniprot.org/citations/10025402http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10025402
http://purl.uniprot.org/citations/10025402http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10025402
http://purl.uniprot.org/citations/10025402http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10025402
http://purl.uniprot.org/citations/10025402http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10025402
http://purl.uniprot.org/uniprot/P63012http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10025402
http://purl.uniprot.org/uniprot/P47709http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10025402