1gje
From Proteopedia
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| - | [[Image:1gje.jpg|left|200px]] | + | [[Image:1gje.jpg|left|200px]] |
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| - | '''Peptide Antagonist of IGFBP-1, Minimized Average Structure''' | + | {{Structure |
| + | |PDB= 1gje |SIZE=350|CAPTION= <scene name='initialview01'>1gje</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Peptide Antagonist of IGFBP-1, Minimized Average Structure''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GJE is a [ | + | 1GJE is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJE OCA]. |
==Reference== | ==Reference== | ||
| - | Structure-function analysis of a phage display-derived peptide that binds to insulin-like growth factor binding protein 1., Skelton NJ, Chen YM, Dubree N, Quan C, Jackson DY, Cochran A, Zobel K, Deshayes K, Baca M, Pisabarro MT, Lowman HB, Biochemistry. 2001 Jul 24;40(29):8487-98. PMID:[http:// | + | Structure-function analysis of a phage display-derived peptide that binds to insulin-like growth factor binding protein 1., Skelton NJ, Chen YM, Dubree N, Quan C, Jackson DY, Cochran A, Zobel K, Deshayes K, Baca M, Pisabarro MT, Lowman HB, Biochemistry. 2001 Jul 24;40(29):8487-98. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11456486 11456486] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Chen, Y M.]] | [[Category: Chen, Y M.]] | ||
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[[Category: loop-turn-helix]] | [[Category: loop-turn-helix]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:23:55 2008'' |
Revision as of 09:23, 20 March 2008
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Peptide Antagonist of IGFBP-1, Minimized Average Structure
Overview
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 naive 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.
About this Structure
1GJE is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Structure-function analysis of a phage display-derived peptide that binds to insulin-like growth factor binding protein 1., Skelton NJ, Chen YM, Dubree N, Quan C, Jackson DY, Cochran A, Zobel K, Deshayes K, Baca M, Pisabarro MT, Lowman HB, Biochemistry. 2001 Jul 24;40(29):8487-98. PMID:11456486
Page seeded by OCA on Thu Mar 20 11:23:55 2008
