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http://purl.uniprot.org/citations/12574113http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12574113http://www.w3.org/2000/01/rdf-schema#comment"The enzyme nitric oxide synthase (NOS) is exquisitely regulated in vivo by the Ca(2+) sensor protein calmodulin (CaM) to control production of NO, a key signaling molecule and cytotoxin. The differential activation of NOS isozymes by CaM has remained enigmatic, despite extensive research. Here, the crystallographic structure of Ca(2+)-loaded CaM bound to a 20 residue peptide comprising the endothelial NOS (eNOS) CaM-binding region establishes their individual conformations and intermolecular interactions, and suggests the basis for isozyme-specific differences. The alpha-helical eNOS peptide binds in an antiparallel orientation to CaM through extensive hydrophobic interactions. Unique NOS interactions occur with: (i). the CaM flexible central linker, explaining its importance in NOS activation; and (ii). the CaM C-terminus, explaining the NOS-specific requirement for a bulky, hydrophobic residue at position 144. This binding mode expands mechanisms for CaM-mediated activation, explains eNOS deactivation by Thr495 phosphorylation, and implicates specific hydrophobic residues in the Ca(2+) independence of inducible NOS."xsd:string
http://purl.uniprot.org/citations/12574113http://purl.org/dc/terms/identifier"doi:10.1093/emboj/cdg078"xsd:string
http://purl.uniprot.org/citations/12574113http://purl.uniprot.org/core/author"Arvai A.S."xsd:string
http://purl.uniprot.org/citations/12574113http://purl.uniprot.org/core/author"Tainer J.A."xsd:string
http://purl.uniprot.org/citations/12574113http://purl.uniprot.org/core/author"Aoyagi M."xsd:string
http://purl.uniprot.org/citations/12574113http://purl.uniprot.org/core/author"Getzoff E.D."xsd:string
http://purl.uniprot.org/citations/12574113http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12574113http://purl.uniprot.org/core/name"EMBO J"xsd:string
http://purl.uniprot.org/citations/12574113http://purl.uniprot.org/core/pages"766-775"xsd:string
http://purl.uniprot.org/citations/12574113http://purl.uniprot.org/core/title"Structural basis for endothelial nitric oxide synthase binding to calmodulin."xsd:string
http://purl.uniprot.org/citations/12574113http://purl.uniprot.org/core/volume"22"xsd:string
http://purl.uniprot.org/citations/12574113http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12574113
http://purl.uniprot.org/citations/12574113http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12574113
http://purl.uniprot.org/uniprot/#_A0A1L1STZ4-mappedCitation-12574113http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12574113
http://purl.uniprot.org/uniprot/#_D3YC69-mappedCitation-12574113http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12574113
http://purl.uniprot.org/uniprot/#_P29474-mappedCitation-12574113http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12574113
http://purl.uniprot.org/uniprot/#_P29477-mappedCitation-12574113http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12574113
http://purl.uniprot.org/uniprot/#_P0DP29-mappedCitation-12574113http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12574113
http://purl.uniprot.org/uniprot/P29474http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12574113
http://purl.uniprot.org/uniprot/A0A1L1STZ4http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12574113
http://purl.uniprot.org/uniprot/P29477http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12574113
http://purl.uniprot.org/uniprot/P0DP29http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12574113
http://purl.uniprot.org/uniprot/D3YC69http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12574113