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http://purl.uniprot.org/citations/15014436http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15014436http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15014436http://www.w3.org/2000/01/rdf-schema#comment"Thrombospondins (TSPs) are extracellular regulators of cell-matrix interactions and cell phenotype. The most highly conserved region of all TSPs are the calcium-binding type 3 (T3) repeats and the C-terminal globular domain (CTD). The crystal structure of a cell-binding TSP-1 fragment, spanning three T3 repeats and the CTD, reveals a compact assembly. The T3 repeats lack secondary structure and are organised around a core of calcium ions; two DxDxDGxxDxxD motifs per repeat each encapsulate two calcium ions in a novel arrangement. The CTD forms a lectin-like beta-sandwich and contains four strictly conserved calcium-binding sites. Disruption of the hairpin structure of T3 repeats 6 and 7 decreases protein secretion and stability. The availability for cell attachment of an RGD motif in T3 repeat 7 is modulated by calcium loading. The central architectural role of calcium explains how it is critical for the functions of the TSP C-terminal region. Mutations in the T3 repeats of TSP-5/COMP, which cause two human skeletal disorders, are predicted to disrupt the tertiary structure of the T3-CTD assembly."xsd:string
http://purl.uniprot.org/citations/15014436http://purl.org/dc/terms/identifier"doi:10.1038/sj.emboj.7600166"xsd:string
http://purl.uniprot.org/citations/15014436http://purl.org/dc/terms/identifier"doi:10.1038/sj.emboj.7600166"xsd:string
http://purl.uniprot.org/citations/15014436http://purl.uniprot.org/core/author"Hohenester E."xsd:string
http://purl.uniprot.org/citations/15014436http://purl.uniprot.org/core/author"Hohenester E."xsd:string
http://purl.uniprot.org/citations/15014436http://purl.uniprot.org/core/author"Kvansakul M."xsd:string
http://purl.uniprot.org/citations/15014436http://purl.uniprot.org/core/author"Kvansakul M."xsd:string
http://purl.uniprot.org/citations/15014436http://purl.uniprot.org/core/author"Adams J.C."xsd:string
http://purl.uniprot.org/citations/15014436http://purl.uniprot.org/core/author"Adams J.C."xsd:string
http://purl.uniprot.org/citations/15014436http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15014436http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15014436http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/15014436http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/15014436http://purl.uniprot.org/core/pages"1223-1233"xsd:string
http://purl.uniprot.org/citations/15014436http://purl.uniprot.org/core/pages"1223-1233"xsd:string
http://purl.uniprot.org/citations/15014436http://purl.uniprot.org/core/title"Structure of a thrombospondin C-terminal fragment reveals a novel calcium core in the type 3 repeats."xsd:string
http://purl.uniprot.org/citations/15014436http://purl.uniprot.org/core/title"Structure of a thrombospondin C-terminal fragment reveals a novel calcium core in the type 3 repeats."xsd:string
http://purl.uniprot.org/citations/15014436http://purl.uniprot.org/core/volume"23"xsd:string
http://purl.uniprot.org/citations/15014436http://purl.uniprot.org/core/volume"23"xsd:string
http://purl.uniprot.org/citations/15014436http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15014436
http://purl.uniprot.org/citations/15014436http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15014436
http://purl.uniprot.org/citations/15014436http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15014436
http://purl.uniprot.org/citations/15014436http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15014436