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http://purl.uniprot.org/citations/17997965http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17997965http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17997965http://www.w3.org/2000/01/rdf-schema#comment"Guanylate cyclase-activating proteins (GCAPs) are Ca(2+)-binding proteins myristoylated at the N terminus that regulate guanylate cyclases in photoreceptor cells and belong to the family of neuronal calcium sensors (NCS). Many NCS proteins display a recoverin-like "calcium-myristoyl switch" whereby the myristoyl group, buried inside the protein in the Ca(2+)-free state, becomes fully exposed upon Ca(2+) binding. Here we present a 2.0 A resolution crystal structure of myristoylated GCAP1 with Ca(2+) bound. The acyl group is buried inside Ca(2+)-bound GCAP1. This is in sharp contrast to Ca(2+)-bound recoverin, where the myristoyl group is solvent exposed. Furthermore, we provide direct evidence that the acyl group in GCAP1 remains buried in the Ca(2+)-free state and does not undergo switching. A pronounced kink in the C-terminal helix and the presence of the myristoyl group allow clustering of sequence elements crucial for GCAP1 activity."xsd:string
http://purl.uniprot.org/citations/17997965http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2007.09.013"xsd:string
http://purl.uniprot.org/citations/17997965http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2007.09.013"xsd:string
http://purl.uniprot.org/citations/17997965http://purl.uniprot.org/core/author"Palczewski K."xsd:string
http://purl.uniprot.org/citations/17997965http://purl.uniprot.org/core/author"Palczewski K."xsd:string
http://purl.uniprot.org/citations/17997965http://purl.uniprot.org/core/author"Sousa M.C."xsd:string
http://purl.uniprot.org/citations/17997965http://purl.uniprot.org/core/author"Sousa M.C."xsd:string
http://purl.uniprot.org/citations/17997965http://purl.uniprot.org/core/author"Stephen R."xsd:string
http://purl.uniprot.org/citations/17997965http://purl.uniprot.org/core/author"Stephen R."xsd:string
http://purl.uniprot.org/citations/17997965http://purl.uniprot.org/core/author"Golczak M."xsd:string
http://purl.uniprot.org/citations/17997965http://purl.uniprot.org/core/author"Golczak M."xsd:string
http://purl.uniprot.org/citations/17997965http://purl.uniprot.org/core/author"Bereta G."xsd:string
http://purl.uniprot.org/citations/17997965http://purl.uniprot.org/core/author"Bereta G."xsd:string
http://purl.uniprot.org/citations/17997965http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17997965http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17997965http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/17997965http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/17997965http://purl.uniprot.org/core/pages"1392-1402"xsd:string
http://purl.uniprot.org/citations/17997965http://purl.uniprot.org/core/pages"1392-1402"xsd:string
http://purl.uniprot.org/citations/17997965http://purl.uniprot.org/core/title"Stabilizing function for myristoyl group revealed by the crystal structure of a neuronal calcium sensor, guanylate cyclase-activating protein 1."xsd:string
http://purl.uniprot.org/citations/17997965http://purl.uniprot.org/core/title"Stabilizing function for myristoyl group revealed by the crystal structure of a neuronal calcium sensor, guanylate cyclase-activating protein 1."xsd:string
http://purl.uniprot.org/citations/17997965http://purl.uniprot.org/core/volume"15"xsd:string
http://purl.uniprot.org/citations/17997965http://purl.uniprot.org/core/volume"15"xsd:string