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http://purl.uniprot.org/citations/21288895http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21288895http://www.w3.org/2000/01/rdf-schema#comment"Neuronal calcium sensor (NCS) proteins transduce Ca2+ signals and are highly conserved from yeast to humans. We determined NMR structures of the NCS-1 homolog from fission yeast (Ncs1), which activates a phosphatidylinositol 4-kinase. Ncs1 contains an α-NH2-linked myristoyl group on a long N-terminal arm and four EF-hand motifs, three of which bind Ca2+, assembled into a compact structure. In Ca2+-free Ncs1, the N-terminal arm positions the fatty acyl chain inside a cavity near the C terminus. The C14 end of the myristate is surrounded by residues in the protein core, whereas its amide-linked (C1) end is flanked by residues at the protein surface. In Ca2+-bound Ncs1, the myristoyl group is extruded (Ca2+-myristoyl switch), exposing a prominent patch of hydrophobic residues that specifically contact phosphatidylinositol 4-kinase. The location of the buried myristate and structure of Ca2+-free Ncs1 are quite different from those in other NCS proteins. Thus, a unique remodeling of each NCS protein by its myristoyl group, and Ca2+-dependent unmasking of different residues, may explain how each family member recognizes distinct target proteins."xsd:string
http://purl.uniprot.org/citations/21288895http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m110.208868"xsd:string
http://purl.uniprot.org/citations/21288895http://purl.uniprot.org/core/author"Lim S."xsd:string
http://purl.uniprot.org/citations/21288895http://purl.uniprot.org/core/author"Thorner J."xsd:string
http://purl.uniprot.org/citations/21288895http://purl.uniprot.org/core/author"Ames J.B."xsd:string
http://purl.uniprot.org/citations/21288895http://purl.uniprot.org/core/author"Strahl T."xsd:string
http://purl.uniprot.org/citations/21288895http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21288895http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/21288895http://purl.uniprot.org/core/pages"12565-12577"xsd:string
http://purl.uniprot.org/citations/21288895http://purl.uniprot.org/core/title"Structure of a Ca2+-myristoyl switch protein that controls activation of a phosphatidylinositol 4-kinase in fission yeast."xsd:string
http://purl.uniprot.org/citations/21288895http://purl.uniprot.org/core/volume"286"xsd:string
http://purl.uniprot.org/citations/21288895http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21288895
http://purl.uniprot.org/citations/21288895http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21288895
http://purl.uniprot.org/uniprot/Q09711#attribution-40BEAC93DEF7811A56985CC9B8C4A9C4http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/21288895
http://purl.uniprot.org/uniprot/Q09711#attribution-C24B973413DCC8699FD2001A828A4AE2http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/21288895
http://purl.uniprot.org/uniprot/#_Q09711-mappedCitation-21288895http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21288895
http://purl.uniprot.org/uniprot/Q09711http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21288895