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http://purl.uniprot.org/citations/17305365http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17305365http://www.w3.org/2000/01/rdf-schema#comment"Insulin-like growth factor binding proteins (IGFBPs) modulate the activity and distribution of insulin-like growth factors (IGFs). IGFBP-6 differs from other IGFBPs in being a relatively specific inhibitor of IGF-II actions. Another distinctive feature of IGFBP-6 is its unique N-terminal disulfide linkages; the N-domains of IGFBPs 1-5 contain six disulfides and share a conserved GCGCC motif, but IGFBP-6 lacks the two adjacent cysteines in this motif, so its first three N-terminal disulfide linkages differ from those of the other IGFBPs. The contributions of the N- and C-domains of IGFBP-6 to its IGF binding properties and their structure-function relationships have been characterized in part, but the structure and function of the distinctive N-terminal subdomain of IGFBP-6 are unknown. Here we report the solution structure of a polypeptide corresponding to residues 1-45 of the N-terminal subdomain of IGFBP-6 (NN-BP-6). The extended structure of the N-terminal subdomain of IGFBP-6 is very different from that of the short two-stranded beta-sheet of the N-terminal subdomain of IGFBP-4 and, by implication, the other IGFBPs. NN-BP-6 contains a potential cation-binding motif; lanthanide ion binding was observed, but no significant interaction was found with physiologically relevant metal ions like calcium or magnesium. However, this subdomain of IGFBP-6 has a higher affinity for IGF-II than IGF-I, suggesting that it may contribute to the marked IGF-II binding preference of IGFBP-6. The extended structure and flexibility of this subdomain of IGFBP-6 could play a role in enhancing the rate of ligand association and thereby be significant in IGF recognition."xsd:string
http://purl.uniprot.org/citations/17305365http://purl.org/dc/terms/identifier"doi:10.1021/bi0619876"xsd:string
http://purl.uniprot.org/citations/17305365http://purl.uniprot.org/core/author"Alewood P.F."xsd:string
http://purl.uniprot.org/citations/17305365http://purl.uniprot.org/core/author"Wang C.C."xsd:string
http://purl.uniprot.org/citations/17305365http://purl.uniprot.org/core/author"Wallace J.C."xsd:string
http://purl.uniprot.org/citations/17305365http://purl.uniprot.org/core/author"Norton R.S."xsd:string
http://purl.uniprot.org/citations/17305365http://purl.uniprot.org/core/author"Yao S."xsd:string
http://purl.uniprot.org/citations/17305365http://purl.uniprot.org/core/author"Bansal P.S."xsd:string
http://purl.uniprot.org/citations/17305365http://purl.uniprot.org/core/author"Bach L.A."xsd:string
http://purl.uniprot.org/citations/17305365http://purl.uniprot.org/core/author"Forbes B.E."xsd:string
http://purl.uniprot.org/citations/17305365http://purl.uniprot.org/core/author"Chandrashekaran I.R."xsd:string
http://purl.uniprot.org/citations/17305365http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17305365http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/17305365http://purl.uniprot.org/core/pages"3065-3074"xsd:string
http://purl.uniprot.org/citations/17305365http://purl.uniprot.org/core/title"The N-terminal subdomain of insulin-like growth factor (IGF) binding protein 6. Structure and interaction with IGFs."xsd:string
http://purl.uniprot.org/citations/17305365http://purl.uniprot.org/core/volume"46"xsd:string
http://purl.uniprot.org/citations/17305365http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17305365
http://purl.uniprot.org/citations/17305365http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17305365
http://purl.uniprot.org/uniprot/#_P24592-mappedCitation-17305365http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17305365
http://purl.uniprot.org/uniprot/P24592http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17305365