| http://purl.uniprot.org/citations/12626499 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12626499 | http://www.w3.org/2000/01/rdf-schema#comment | "We have previously reported that two highly conserved amino acids in the C-terminal domain of rat insulin-like growth factor-binding protein (IGFBP)-5, Gly(203) and Gln(209), are involved in binding to insulin-like growth factor (IGF)-1. Here we report that mutagenesis of both amino acids simultaneously (C-Term mutant) results in a cumulative effect and an even greater reduction in IGF-I binding: 30-fold measured by solution phase IGF binding assay and 10-fold by biosensor analysis. We compared these reductions in ligand binding to the effects of specific mutations of five amino acids in the N-terminal domain (N-Term mutant), which had previously been shown by others to cause a very large reduction in IGF-I binding (). Our results confirm this as the major IGF-binding site. To prove that the mutations in either N- or C-Term were specific for IGF-I binding, we carried out CD spectroscopy and showed that these alterations did not lead to gross conformational changes in protein structure for either mutant. Combining these mutations in both domains (N+C-Term mutant) has a cumulative effect and leads to a 126-fold reduction in IGF-I binding as measured by biosensor. Furthermore, the equivalent mutations in the C terminus of rat IGFBP-2 (C-Term 2) also results in a significant reduction in IGF-I binding, suggesting that the highly conserved Gly and Gln residues have a conserved IGF-I binding function in all six IGFBPs. Finally, although these residues lie within a major heparin-binding site in IGFBP-5 and -3, we also show that the mutations in C-Term have no effect on heparin binding."xsd:string |
| http://purl.uniprot.org/citations/12626499 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m300526200"xsd:string |
| http://purl.uniprot.org/citations/12626499 | http://purl.uniprot.org/core/author | "Phillips K."xsd:string |
| http://purl.uniprot.org/citations/12626499 | http://purl.uniprot.org/core/author | "Song H."xsd:string |
| http://purl.uniprot.org/citations/12626499 | http://purl.uniprot.org/core/author | "Kelly S.M."xsd:string |
| http://purl.uniprot.org/citations/12626499 | http://purl.uniprot.org/core/author | "Beattie J."xsd:string |
| http://purl.uniprot.org/citations/12626499 | http://purl.uniprot.org/core/author | "Allan G.J."xsd:string |
| http://purl.uniprot.org/citations/12626499 | http://purl.uniprot.org/core/author | "Flint D.J."xsd:string |
| http://purl.uniprot.org/citations/12626499 | http://purl.uniprot.org/core/author | "Shand J.H."xsd:string |
| http://purl.uniprot.org/citations/12626499 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12626499 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/12626499 | http://purl.uniprot.org/core/pages | "17859-17866"xsd:string |
| http://purl.uniprot.org/citations/12626499 | http://purl.uniprot.org/core/title | "Specific amino acid substitutions determine the differential contribution of the N- and C-terminal domains of insulin-like growth factor (IGF)-binding protein-5 in binding IGF-I."xsd:string |
| http://purl.uniprot.org/citations/12626499 | http://purl.uniprot.org/core/volume | "278"xsd:string |
| http://purl.uniprot.org/citations/12626499 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12626499 |
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| http://purl.uniprot.org/uniprot/#_A6IFM2-mappedCitation-12626499 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/12626499 |
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| http://purl.uniprot.org/uniprot/#_A6IFM7-mappedCitation-12626499 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/12626499 |