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1kvg

From Proteopedia

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{{STRUCTURE_1kvg| PDB=1kvg | SCENE= }}
{{STRUCTURE_1kvg| PDB=1kvg | SCENE= }}
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'''EPO-3 beta Hairpin Peptide'''
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===EPO-3 beta Hairpin Peptide===
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==Overview==
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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).
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(as it appears on PubMed at http://www.pubmed.gov), where 11884148 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11884148}}
==About this Structure==
==About this Structure==
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KVG OCA].
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Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KVG OCA].
==Reference==
==Reference==
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[[Category: Skelton, N J.]]
[[Category: Skelton, N J.]]
[[Category: Beta hairpin peptide]]
[[Category: Beta hairpin peptide]]
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Revision as of 08:05, 2 July 2008

Image:1kvg.png

Template:STRUCTURE 1kvg

EPO-3 beta Hairpin Peptide

Template:ABSTRACT PUBMED 11884148

About this Structure

Full experimental 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 Wed Jul 2 11:05:24 2008

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