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http://purl.uniprot.org/citations/15642270http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15642270http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15642270http://www.w3.org/2000/01/rdf-schema#comment"Insulin-like growth factor binding proteins (IGFBPs) control the extracellular distribution, function, and activity of IGFs. Here, we report an X-ray structure of the binary complex of IGF-I and the N-terminal domain of IGFBP-4 (NBP-4, residues 3-82) and a model of the ternary complex of IGF-I, NBP-4, and the C-terminal domain (CBP-4, residues 151-232) derived from diffraction data with weak definition of the C-terminal domain. These structures show how the IGFBPs regulate IGF signaling. Key features of the structures include (1) a disulphide bond ladder that binds to IGF and partially masks the IGF residues responsible for type 1 IGF receptor (IGF-IR) binding, (2) the high-affinity IGF-I interaction site formed by residues 39-82 in a globular fold, and (3) CBP-4 interactions. Although CBP-4 does not bind individually to either IGF-I or NBP-4, in the ternary complex, CBP-4 contacts both and also blocks the IGF-IR binding region of IGF-I."xsd:string
http://purl.uniprot.org/citations/15642270http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2004.11.009"xsd:string
http://purl.uniprot.org/citations/15642270http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2004.11.009"xsd:string
http://purl.uniprot.org/citations/15642270http://purl.uniprot.org/core/author"Huber R."xsd:string
http://purl.uniprot.org/citations/15642270http://purl.uniprot.org/core/author"Huber R."xsd:string
http://purl.uniprot.org/citations/15642270http://purl.uniprot.org/core/author"Holak T.A."xsd:string
http://purl.uniprot.org/citations/15642270http://purl.uniprot.org/core/author"Holak T.A."xsd:string
http://purl.uniprot.org/citations/15642270http://purl.uniprot.org/core/author"Engh R.A."xsd:string
http://purl.uniprot.org/citations/15642270http://purl.uniprot.org/core/author"Engh R.A."xsd:string
http://purl.uniprot.org/citations/15642270http://purl.uniprot.org/core/author"Lang K."xsd:string
http://purl.uniprot.org/citations/15642270http://purl.uniprot.org/core/author"Lang K."xsd:string
http://purl.uniprot.org/citations/15642270http://purl.uniprot.org/core/author"Wisniewska M."xsd:string
http://purl.uniprot.org/citations/15642270http://purl.uniprot.org/core/author"Wisniewska M."xsd:string
http://purl.uniprot.org/citations/15642270http://purl.uniprot.org/core/author"Popowicz G.M."xsd:string
http://purl.uniprot.org/citations/15642270http://purl.uniprot.org/core/author"Popowicz G.M."xsd:string
http://purl.uniprot.org/citations/15642270http://purl.uniprot.org/core/author"Kuenkele K.-P."xsd:string
http://purl.uniprot.org/citations/15642270http://purl.uniprot.org/core/author"Kuenkele K.-P."xsd:string
http://purl.uniprot.org/citations/15642270http://purl.uniprot.org/core/author"Siwanowicz I."xsd:string
http://purl.uniprot.org/citations/15642270http://purl.uniprot.org/core/author"Siwanowicz I."xsd:string
http://purl.uniprot.org/citations/15642270http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15642270http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15642270http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/15642270http://purl.uniprot.org/core/name"Structure"xsd:string