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http://purl.uniprot.org/citations/11533490http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11533490http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11533490http://www.w3.org/2000/01/rdf-schema#comment"Natriuretic peptides (NPs) are vasoactive cyclic-peptide hormones important in blood pressure regulation through interaction with natriuretic cell-surface receptors. We report the hormone-binding thermodynamics and crystal structures at 2.9 and 2.0 angstroms, respectively, of the extracellular domain of the unliganded human NP receptor (NPR-C) and its complex with CNP, a 22-amino acid NP. A single CNP molecule is bound in the interface of an NPR-C dimer, resulting in asymmetric interactions between the hormone and the symmetrically related receptors. Hormone binding induces a 20 angstrom closure between the membrane-proximal domains of the dimer. In each monomer, the opening of an interdomain cleft, which is tethered together by a linker peptide acting as a molecular spring, is likely a conserved allosteric trigger for intracellular signaling by the natriuretic receptor family."xsd:string
http://purl.uniprot.org/citations/11533490http://purl.org/dc/terms/identifier"doi:10.1126/science.1062246"xsd:string
http://purl.uniprot.org/citations/11533490http://purl.org/dc/terms/identifier"doi:10.1126/science.1062246"xsd:string
http://purl.uniprot.org/citations/11533490http://purl.uniprot.org/core/author"Garcia K.C."xsd:string
http://purl.uniprot.org/citations/11533490http://purl.uniprot.org/core/author"Garcia K.C."xsd:string
http://purl.uniprot.org/citations/11533490http://purl.uniprot.org/core/author"He X.-L."xsd:string
http://purl.uniprot.org/citations/11533490http://purl.uniprot.org/core/author"He X.-L."xsd:string
http://purl.uniprot.org/citations/11533490http://purl.uniprot.org/core/author"Chow D.-C."xsd:string
http://purl.uniprot.org/citations/11533490http://purl.uniprot.org/core/author"Chow D.-C."xsd:string
http://purl.uniprot.org/citations/11533490http://purl.uniprot.org/core/author"Martick M.M."xsd:string
http://purl.uniprot.org/citations/11533490http://purl.uniprot.org/core/author"Martick M.M."xsd:string
http://purl.uniprot.org/citations/11533490http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11533490http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11533490http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/11533490http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/11533490http://purl.uniprot.org/core/pages"1657-1662"xsd:string
http://purl.uniprot.org/citations/11533490http://purl.uniprot.org/core/pages"1657-1662"xsd:string
http://purl.uniprot.org/citations/11533490http://purl.uniprot.org/core/title"Allosteric activation of a spring-loaded natriuretic peptide receptor dimer by hormone."xsd:string
http://purl.uniprot.org/citations/11533490http://purl.uniprot.org/core/title"Allosteric activation of a spring-loaded natriuretic peptide receptor dimer by hormone."xsd:string
http://purl.uniprot.org/citations/11533490http://purl.uniprot.org/core/volume"293"xsd:string
http://purl.uniprot.org/citations/11533490http://purl.uniprot.org/core/volume"293"xsd:string
http://purl.uniprot.org/citations/11533490http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11533490
http://purl.uniprot.org/citations/11533490http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11533490