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http://purl.uniprot.org/citations/31278385http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31278385http://www.w3.org/2000/01/rdf-schema#comment"The high-conductance intracellular calcium (Ca2+) channel RyR2 is essential for the coupling of excitation and contraction in cardiac muscle. Among various modulators, calmodulin (CaM) regulates RyR2 in a Ca2+-dependent manner. Here we reveal the regulatory mechanism by which porcine RyR2 is modulated by human CaM through the structural determination of RyR2 under eight conditions. Apo-CaM and Ca2+-CaM bind to distinct but overlapping sites in an elongated cleft formed by the handle, helical and central domains. The shift in CaM-binding sites on RyR2 is controlled by Ca2+ binding to CaM, rather than to RyR2. Ca2+-CaM induces rotations and intradomain shifts of individual central domains, resulting in pore closure of the PCB95 and Ca2+-activated channel. By contrast, the pore of the ATP, caffeine and Ca2+-activated channel remains open in the presence of Ca2+-CaM, which suggests that Ca2+-CaM is one of the many competing modulators of RyR2 gating."xsd:string
http://purl.uniprot.org/citations/31278385http://purl.org/dc/terms/identifier"doi:10.1038/s41586-019-1377-y"xsd:string
http://purl.uniprot.org/citations/31278385http://purl.uniprot.org/core/author"Huang G."xsd:string
http://purl.uniprot.org/citations/31278385http://purl.uniprot.org/core/author"Zhang L."xsd:string
http://purl.uniprot.org/citations/31278385http://purl.uniprot.org/core/author"Wang R."xsd:string
http://purl.uniprot.org/citations/31278385http://purl.uniprot.org/core/author"Wei J."xsd:string
http://purl.uniprot.org/citations/31278385http://purl.uniprot.org/core/author"Zhou G."xsd:string
http://purl.uniprot.org/citations/31278385http://purl.uniprot.org/core/author"Chi X."xsd:string
http://purl.uniprot.org/citations/31278385http://purl.uniprot.org/core/author"Lei J."xsd:string
http://purl.uniprot.org/citations/31278385http://purl.uniprot.org/core/author"Yan N."xsd:string
http://purl.uniprot.org/citations/31278385http://purl.uniprot.org/core/author"Gong D."xsd:string
http://purl.uniprot.org/citations/31278385http://purl.uniprot.org/core/author"Chen S.R.W."xsd:string
http://purl.uniprot.org/citations/31278385http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/31278385http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/31278385http://purl.uniprot.org/core/pages"347-351"xsd:string
http://purl.uniprot.org/citations/31278385http://purl.uniprot.org/core/title"Modulation of cardiac ryanodine receptor 2 by calmodulin."xsd:string
http://purl.uniprot.org/citations/31278385http://purl.uniprot.org/core/volume"572"xsd:string
http://purl.uniprot.org/citations/31278385http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/31278385
http://purl.uniprot.org/citations/31278385http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/31278385
http://purl.uniprot.org/uniprot/#_B4DJ51-mappedCitation-31278385http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31278385
http://purl.uniprot.org/uniprot/#_P0DP23-mappedCitation-31278385http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31278385
http://purl.uniprot.org/uniprot/#_P0DP24-mappedCitation-31278385http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31278385
http://purl.uniprot.org/uniprot/#_P0DP25-mappedCitation-31278385http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31278385
http://purl.uniprot.org/uniprot/#_P68106-mappedCitation-31278385http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31278385