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http://purl.uniprot.org/citations/11224573http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11224573http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11224573http://www.w3.org/2000/01/rdf-schema#comment"Syntaxins and Sec1/munc18 proteins are central to intracellular membrane fusion. All syntaxins comprise a variable N-terminal region, a conserved SNARE motif that is critical for SNARE complex formation, and a transmembrane region. The N-terminal region of neuronal syntaxin 1A contains a three-helix domain that folds back onto the SNARE motif forming a 'closed' conformation; this conformation is required for munc18-1 binding. We have examined the generality of the structural properties of syntaxins by NMR analysis of Vam3p, a yeast syntaxin essential for vacuolar fusion. Surprisingly, Vam3p also has an N-terminal three-helical domain despite lacking apparent sequence homology with syntaxin 1A in this region. However, Vam3p does not form a closed conformation and its N-terminal domain is not required for binding to the Sec1/munc18 protein Vps33p, suggesting that critical distinctions exist in the mechanisms used by syntaxins to govern different types of membrane fusion."xsd:string
http://purl.uniprot.org/citations/11224573http://purl.org/dc/terms/identifier"doi:10.1038/85012"xsd:string
http://purl.uniprot.org/citations/11224573http://purl.org/dc/terms/identifier"doi:10.1038/85012"xsd:string
http://purl.uniprot.org/citations/11224573http://purl.uniprot.org/core/author"Suedhof T.C."xsd:string
http://purl.uniprot.org/citations/11224573http://purl.uniprot.org/core/author"Suedhof T.C."xsd:string
http://purl.uniprot.org/citations/11224573http://purl.uniprot.org/core/author"Wang Y."xsd:string
http://purl.uniprot.org/citations/11224573http://purl.uniprot.org/core/author"Wang Y."xsd:string
http://purl.uniprot.org/citations/11224573http://purl.uniprot.org/core/author"Yamaguchi T."xsd:string
http://purl.uniprot.org/citations/11224573http://purl.uniprot.org/core/author"Yamaguchi T."xsd:string
http://purl.uniprot.org/citations/11224573http://purl.uniprot.org/core/author"Dulubova I."xsd:string
http://purl.uniprot.org/citations/11224573http://purl.uniprot.org/core/author"Dulubova I."xsd:string
http://purl.uniprot.org/citations/11224573http://purl.uniprot.org/core/author"Rizo J."xsd:string
http://purl.uniprot.org/citations/11224573http://purl.uniprot.org/core/author"Rizo J."xsd:string
http://purl.uniprot.org/citations/11224573http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11224573http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11224573http://purl.uniprot.org/core/name"Nat. Struct. Biol."xsd:string
http://purl.uniprot.org/citations/11224573http://purl.uniprot.org/core/name"Nat. Struct. Biol."xsd:string
http://purl.uniprot.org/citations/11224573http://purl.uniprot.org/core/pages"258-264"xsd:string
http://purl.uniprot.org/citations/11224573http://purl.uniprot.org/core/pages"258-264"xsd:string
http://purl.uniprot.org/citations/11224573http://purl.uniprot.org/core/title"Vam3p structure reveals conserved and divergent properties of syntaxins."xsd:string
http://purl.uniprot.org/citations/11224573http://purl.uniprot.org/core/title"Vam3p structure reveals conserved and divergent properties of syntaxins."xsd:string
http://purl.uniprot.org/citations/11224573http://purl.uniprot.org/core/volume"8"xsd:string
http://purl.uniprot.org/citations/11224573http://purl.uniprot.org/core/volume"8"xsd:string