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http://purl.uniprot.org/citations/16186819http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16186819http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16186819http://www.w3.org/2000/01/rdf-schema#comment"Thrombospondins (THBSs) are secreted glycoproteins that have key roles in interactions between cells and the extracellular matrix. Here, we describe the 2.6-A-resolution crystal structure of the glycosylated signature domain of human THBS2, which includes three epidermal growth factor-like modules, 13 aspartate-rich repeats and a lectin-like module. These elements interact extensively to form three structural regions termed the stalk, wire and globe. The THBS2 signature domain is stabilized by these interactions and by a network of 30 bound Ca(2+) ions and 18 disulfide bonds. The structure suggests how genetic alterations of THBSs result in disease."xsd:string
http://purl.uniprot.org/citations/16186819http://purl.org/dc/terms/identifier"doi:10.1038/nsmb997"xsd:string
http://purl.uniprot.org/citations/16186819http://purl.org/dc/terms/identifier"doi:10.1038/nsmb997"xsd:string
http://purl.uniprot.org/citations/16186819http://purl.uniprot.org/core/author"Keck J.L."xsd:string
http://purl.uniprot.org/citations/16186819http://purl.uniprot.org/core/author"Keck J.L."xsd:string
http://purl.uniprot.org/citations/16186819http://purl.uniprot.org/core/author"Bernstein D.A."xsd:string
http://purl.uniprot.org/citations/16186819http://purl.uniprot.org/core/author"Bernstein D.A."xsd:string
http://purl.uniprot.org/citations/16186819http://purl.uniprot.org/core/author"Mosher D.F."xsd:string
http://purl.uniprot.org/citations/16186819http://purl.uniprot.org/core/author"Mosher D.F."xsd:string
http://purl.uniprot.org/citations/16186819http://purl.uniprot.org/core/author"Annis D.S."xsd:string
http://purl.uniprot.org/citations/16186819http://purl.uniprot.org/core/author"Annis D.S."xsd:string
http://purl.uniprot.org/citations/16186819http://purl.uniprot.org/core/author"Carlson C.B."xsd:string
http://purl.uniprot.org/citations/16186819http://purl.uniprot.org/core/author"Carlson C.B."xsd:string
http://purl.uniprot.org/citations/16186819http://purl.uniprot.org/core/author"Hannah B.L."xsd:string
http://purl.uniprot.org/citations/16186819http://purl.uniprot.org/core/author"Hannah B.L."xsd:string
http://purl.uniprot.org/citations/16186819http://purl.uniprot.org/core/author"Misenheimer T.M."xsd:string
http://purl.uniprot.org/citations/16186819http://purl.uniprot.org/core/author"Misenheimer T.M."xsd:string
http://purl.uniprot.org/citations/16186819http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16186819http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16186819http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/16186819http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/16186819http://purl.uniprot.org/core/pages"910-914"xsd:string
http://purl.uniprot.org/citations/16186819http://purl.uniprot.org/core/pages"910-914"xsd:string