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| | {{STRUCTURE_1kvg| PDB=1kvg | SCENE= }} | | {{STRUCTURE_1kvg| PDB=1kvg | SCENE= }} |
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| - | '''EPO-3 beta Hairpin Peptide'''
| + | ===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).
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11884148}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11884148 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11884148}} |
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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]. | + | Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KVG OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Skelton, N J.]] | | [[Category: Skelton, N J.]] |
| | [[Category: Beta hairpin peptide]] | | [[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 Wed Jul 2 11:05:24 2008'' |
Revision as of 08:05, 2 July 2008
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
