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1kat

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{{STRUCTURE_1kat| PDB=1kat | SCENE= }}
{{STRUCTURE_1kat| PDB=1kat | SCENE= }}
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'''Solution Structure of a Phage-Derived Peptide Antagonist in Complex with Vascular Endothelial Growth Factor'''
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===Solution Structure of a Phage-Derived Peptide Antagonist in Complex with Vascular Endothelial Growth Factor===
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==Overview==
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Vascular endothelial growth factor (VEGF) is a potent endothelial cell-specific mediator of angiogenesis and vasculogenesis. VEGF is involved pathologically in cancer, proliferative retinopathy and rheumatoid arthritis, and as such represents an important therapeutic target. Three classes of disulfide-constrained peptides that antagonize binding of the VEGF dimer to its receptors, KDR and Flt-1, were identified previously using phage display methods. NMR studies of a representative peptide from the most potent class of these peptide antagonists, v107 (GGNECDAIRMWEWECFERL), were undertaken to characterize its interactions with VEGF. v107 has no defined structure free in solution, but binding to VEGF induces folding of the peptide. The solution structure of the VEGF receptor-binding domain-v107 complex was determined using 3940 (1970 per VEGF monomer) internuclear distance and 476 (238 per VEGF monomer) dihedral angle restraints derived from NMR data obtained using samples containing either (13)C/(15)N-labeled protein plus excess unlabeled peptide or (13)C/(15)N-labeled peptide plus excess unlabeled protein. Residual dipolar coupling restraints supplemented the structure determination of the complex and were found to increase significantly both the global precision of VEGF in the complex and the agreement with available crystal structures of VEGF. The calculated ensemble of structures is of high precision and is in excellent agreement with the experimental restraints. v107 has a turn-helix conformation with hydrophobic residues partitioned to one face of the peptide and polar or charged residues at the other face. Contacts between two v107 peptides and the VEGF dimer are mediated by primarily hydrophobic side-chain interactions. The v107-binding site on VEGF overlaps partially with the binding site of KDR and is similar to that for domain 2 of Flt-1. The structure of the VEGF-v107 complex provides new insight into how binding to VEGF can be achieved that may be useful for the design of small molecule antagonists.
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(as it appears on PubMed at http://www.pubmed.gov), where 11866530 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11866530}}
==About this Structure==
==About this Structure==
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1KAT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KAT OCA].
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1KAT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KAT OCA].
==Reference==
==Reference==
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[[Category: Homodimer]]
[[Category: Homodimer]]
[[Category: Protein-peptide complex]]
[[Category: Protein-peptide complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:30:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:03:08 2008''

Revision as of 07:03, 2 July 2008

Image:1kat.png

Template:STRUCTURE 1kat

Solution Structure of a Phage-Derived Peptide Antagonist in Complex with Vascular Endothelial Growth Factor

Template:ABSTRACT PUBMED 11866530

About this Structure

1KAT is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Solution structure of a phage-derived peptide antagonist in complex with vascular endothelial growth factor., Pan B, Li B, Russell SJ, Tom JY, Cochran AG, Fairbrother WJ, J Mol Biol. 2002 Feb 22;316(3):769-87. PMID:11866530

Page seeded by OCA on Wed Jul 2 10:03:08 2008

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