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1kvg
From Proteopedia
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| - | [[Image:1kvg.gif|left|200px]] | + | [[Image:1kvg.gif|left|200px]] |
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| - | '''EPO-3 beta Hairpin Peptide''' | + | {{Structure |
| + | |PDB= 1kvg |SIZE=350|CAPTION= <scene name='initialview01'>1kvg</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''EPO-3 beta Hairpin Peptide''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1KVG is a [ | + | 1KVG 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=1KVG OCA]. |
==Reference== | ==Reference== | ||
| - | Amino acid determinants of beta-hairpin conformation in erythropoeitin receptor agonist peptides derived from a phage display library., Skelton NJ, Russell S, de Sauvage F, Cochran AG, J Mol Biol. 2002 Mar 8;316(5):1111-25. PMID:[http:// | + | Amino acid determinants of beta-hairpin conformation in erythropoeitin receptor agonist peptides derived from a phage display library., Skelton NJ, Russell S, de Sauvage F, Cochran AG, J Mol Biol. 2002 Mar 8;316(5):1111-25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11884148 11884148] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Cochran, A G.]] | [[Category: Cochran, A G.]] | ||
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[[Category: beta hairpin peptide]] | [[Category: beta hairpin peptide]] | ||
| - | ''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 12:22:37 2008'' |
Revision as of 10:22, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
EPO-3 beta Hairpin Peptide
Overview
Display of peptide libraries on filamentous phage has led to the identification of peptides of the form X(2-5)CX(2)GPXTWXCX(2-5) (where X is a variable residue) that bind to the extra-cellular portion of the erythropoietin receptor (EPO-R). These peptides adopt beta-hairpin conformations when co-crystallized with EPO-R. Solution NMR studies reveal that the peptide is conformationally heterogeneous in the absence of receptor due to cis-trans isomerization about the Gly-Pro peptide bond. Replacement of the conserved threonine residue with glycine at the turn i+3 position produces a stable beta-hairpin conformation in solution, although this peptide no longer has activity in an EPO-R-dependent cell proliferation assay. A truncated form of the EPO-R-binding peptide (containing the i+3 glycine residue) also forms a highly populated, monomeric beta-hairpin. In contrast, phage-derived peptide antagonists of insulin-like growth factor binding protein 1 (IGFBP-1) have a high level of sequence identity with the truncated EPO-R peptide (eight of 12 residues) yet adopt a turn-alpha-helix conformation in solution. Peptides containing all possible pairwise amino acid substitutions between the EPO-R and IGFBP-1 peptides have been analyzed to assess the degree to which the non-conserved residues stabilize the hairpin or helix conformation. All four residues present in the original sequence are required for maximum population of either the beta-hairpin or alpha-helix conformation, although some substitutions have a more dominant effect. The results demonstrate that, within a given sequence, the observed conformation can be dictated by a small subset of the residues (in this case four out of 12).
About this Structure
1KVG is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Amino acid determinants of beta-hairpin conformation in erythropoeitin receptor agonist peptides derived from a phage display library., Skelton NJ, Russell S, de Sauvage F, Cochran AG, J Mol Biol. 2002 Mar 8;316(5):1111-25. PMID:11884148
Page seeded by OCA on Thu Mar 20 12:22:37 2008
