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http://purl.uniprot.org/citations/26703466http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26703466http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26703466http://www.w3.org/2000/01/rdf-schema#comment"GCAP1, a member of the neuronal calcium sensor subclass of the calmodulin superfamily, confers Ca(2+)-sensitive activation of retinal guanylyl cyclase 1 (RetGC1). We present NMR resonance assignments, residual dipolar coupling data, functional analysis, and a structural model of GCAP1 mutant (GCAP1(V77E)) in the Ca(2+)-free/Mg(2+)-bound state. NMR chemical shifts and residual dipolar coupling data reveal Ca(2+)-dependent differences for residues 170-174. An NMR-derived model of GCAP1(V77E) contains Mg(2+) bound at EF2 and looks similar to Ca(2+) saturated GCAP1 (root mean square deviations = 2.0 Å). Ca(2+)-dependent structural differences occur in the fourth EF-hand (EF4) and adjacent helical region (residues 164-174 called the Ca(2+) switch helix). Ca(2+)-induced shortening of the Ca(2+) switch helix changes solvent accessibility of Thr-171 and Leu-174 that affects the domain interface. Although the Ca(2+) switch helix is not part of the RetGC1 binding site, insertion of an extra Gly residue between Ser-173 and Leu-174 as well as deletion of Arg-172, Ser-173, or Leu-174 all caused a decrease in Ca(2+) binding affinity and abolished RetGC1 activation. We conclude that Ca(2+)-dependent conformational changes in the Ca(2+) switch helix are important for activating RetGC1 and provide further support for a Ca(2+)-myristoyl tug mechanism."xsd:string
http://purl.uniprot.org/citations/26703466http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m115.696161"xsd:string
http://purl.uniprot.org/citations/26703466http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m115.696161"xsd:string
http://purl.uniprot.org/citations/26703466http://purl.uniprot.org/core/author"Lim S."xsd:string
http://purl.uniprot.org/citations/26703466http://purl.uniprot.org/core/author"Lim S."xsd:string
http://purl.uniprot.org/citations/26703466http://purl.uniprot.org/core/author"Ames J.B."xsd:string
http://purl.uniprot.org/citations/26703466http://purl.uniprot.org/core/author"Ames J.B."xsd:string
http://purl.uniprot.org/citations/26703466http://purl.uniprot.org/core/author"Dizhoor A.M."xsd:string
http://purl.uniprot.org/citations/26703466http://purl.uniprot.org/core/author"Dizhoor A.M."xsd:string
http://purl.uniprot.org/citations/26703466http://purl.uniprot.org/core/author"Olshevskaya E.V."xsd:string
http://purl.uniprot.org/citations/26703466http://purl.uniprot.org/core/author"Olshevskaya E.V."xsd:string
http://purl.uniprot.org/citations/26703466http://purl.uniprot.org/core/author"Peshenko I.V."xsd:string
http://purl.uniprot.org/citations/26703466http://purl.uniprot.org/core/author"Peshenko I.V."xsd:string
http://purl.uniprot.org/citations/26703466http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/26703466http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/26703466http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/26703466http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/26703466http://purl.uniprot.org/core/pages"4429-4441"xsd:string
http://purl.uniprot.org/citations/26703466http://purl.uniprot.org/core/pages"4429-4441"xsd:string
http://purl.uniprot.org/citations/26703466http://purl.uniprot.org/core/title"Structure of guanylyl cyclase activator protein 1 (GCAP1) mutant V77E in a Ca2+-free/Mg2+-bound activator state."xsd:string
http://purl.uniprot.org/citations/26703466http://purl.uniprot.org/core/title"Structure of guanylyl cyclase activator protein 1 (GCAP1) mutant V77E in a Ca2+-free/Mg2+-bound activator state."xsd:string
http://purl.uniprot.org/citations/26703466http://purl.uniprot.org/core/volume"291"xsd:string
http://purl.uniprot.org/citations/26703466http://purl.uniprot.org/core/volume"291"xsd:string