| pubmed-article:11456486 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11456486 | lifeskim:mentions | umls-concept:C0004651 | lld:lifeskim |
| pubmed-article:11456486 | lifeskim:mentions | umls-concept:C0074825 | lld:lifeskim |
| pubmed-article:11456486 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:11456486 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:11456486 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:11456486 | pubmed:issue | 29 | lld:pubmed |
| pubmed-article:11456486 | pubmed:dateCreated | 2001-7-17 | lld:pubmed |
| pubmed-article:11456486 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11456486 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11456486 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11456486 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11456486 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11456486 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11456486 | pubmed:abstractText | Highly structured, peptide antagonists of the interaction between insulin-like growth factor 1 (IGF-I) and IGF binding protein 1 (IGFBP-1) have recently been discovered by phage display of naïve peptide libraries [Lowman, H. B., et al. (1998) Biochemistry 37, 8870--8878]. We now report a detailed analysis of the features of this turn-helix peptide motif that are necessary for IGFBP-1 binding and structural integrity. Further rounds of phage randomization indicate the importance of residues contributing to a hydrophobic patch on one face of the helix. Alanine-scanning substitutions confirm that the hydrophobic residues are necessary for binding. However, structural analysis by NMR spectroscopy indicates that some of these analogues are less well folded. Structured, high-affinity analogues that lack the disulfide bond were prepared by introducing a covalent constraint between side chains at positions i and i + 7 or i + 8 within the helix. Analogues based on this scaffold demonstrate that a helical conformation is present in the bound state, and that hydrophobic side chains in this helix, and residues immediately preceding it, interact with IGFBP-1. By comparison of alanine scanning data for IGF-I and the turn-helix peptide, we propose a model for common surface features of these molecules that recognize IGFBP-1. | lld:pubmed |
| pubmed-article:11456486 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11456486 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11456486 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11456486 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11456486 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11456486 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11456486 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11456486 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11456486 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11456486 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:11456486 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:11456486 | pubmed:author | pubmed-author:ChenY MYM | lld:pubmed |
| pubmed-article:11456486 | pubmed:author | pubmed-author:TingY CYC | lld:pubmed |
| pubmed-article:11456486 | pubmed:author | pubmed-author:ZobelKK | lld:pubmed |
| pubmed-article:11456486 | pubmed:author | pubmed-author:SkeltonN JNJ | lld:pubmed |
| pubmed-article:11456486 | pubmed:author | pubmed-author:LowmanH BHB | lld:pubmed |
| pubmed-article:11456486 | pubmed:author | pubmed-author:PisabarroM... | lld:pubmed |
| pubmed-article:11456486 | pubmed:author | pubmed-author:BacaMM | lld:pubmed |
| pubmed-article:11456486 | pubmed:author | pubmed-author:JacksonD YDY | lld:pubmed |
| pubmed-article:11456486 | pubmed:author | pubmed-author:CochranAA | lld:pubmed |
| pubmed-article:11456486 | pubmed:author | pubmed-author:DubreeNN | lld:pubmed |
| pubmed-article:11456486 | pubmed:author | pubmed-author:DeshayesKK | lld:pubmed |
| pubmed-article:11456486 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11456486 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:11456486 | pubmed:volume | 40 | lld:pubmed |
| pubmed-article:11456486 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11456486 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11456486 | pubmed:pagination | 8487-98 | lld:pubmed |
| pubmed-article:11456486 | pubmed:dateRevised | 2005-11-17 | lld:pubmed |
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| pubmed-article:11456486 | pubmed:meshHeading | pubmed-meshheading:11456486... | lld:pubmed |
| pubmed-article:11456486 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11456486 | pubmed:articleTitle | Structure-function analysis of a phage display-derived peptide that binds to insulin-like growth factor binding protein 1. | lld:pubmed |
| pubmed-article:11456486 | pubmed:affiliation | Department of Protein Engineering, Genentech, Inc., 1 DNA Way, South San Francisco, California 94080, USA. skelly@gene.com | lld:pubmed |
| pubmed-article:11456486 | pubmed:publicationType | Journal Article | lld:pubmed |
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