1kvg
From Proteopedia
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[[Image:1kvg.gif|left|200px]] | [[Image:1kvg.gif|left|200px]] | ||
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| - | + | {{STRUCTURE_1kvg| PDB=1kvg | SCENE= }} | |
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'''EPO-3 beta Hairpin Peptide''' | '''EPO-3 beta Hairpin Peptide''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | 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://www.ncbi.nlm.nih.gov/pubmed/11884148 11884148] | 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: Cochran, A G.]] | [[Category: Cochran, A G.]] | ||
[[Category: Russell, S.]] | [[Category: Russell, S.]] | ||
[[Category: Sauvage, F de.]] | [[Category: Sauvage, F de.]] | ||
[[Category: Skelton, N J.]] | [[Category: Skelton, N J.]] | ||
| - | [[Category: | + | [[Category: Beta hairpin peptide]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:13:05 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 20:13, 2 May 2008
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
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 Fri May 2 23:13:05 2008
