1lb7: Difference between revisions

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|ACTIVITY=  
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lb7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lb7 OCA], [http://www.ebi.ac.uk/pdbsum/1lb7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lb7 RCSB]</span>
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[[Category: peptide]]
[[Category: peptide]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:28:52 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:00:36 2008''

Revision as of 19:00, 30 March 2008

File:1lb7.jpg


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1lb7
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



IGF-F1-1, A PEPTIDE ANTAGONIST OF IGF-1


Overview

A panel of 22 naive peptide libraries was constructed in a polyvalent phage display format and sorted against insulin-like growth factor-1 (IGF-1). The libraries were pooled to achieve a total diversity of 4.4 x 10(11). After three rounds of selection, the majority of the phage clones bound specifically to IGF-1, with a disulfide-constrained CX(9)C scaffold dominating the selection. Four monovalently displayed sub-libraries were designed on the basis of these conserved motifs. Sub-library maturation in a monovalent format yielded an antagonistic peptide that inhibited the interactions between IGF-1 and two cell-surface receptors and those between IGF-1 and two soluble IGF binding proteins with micromolar potency. NMR analysis revealed that the peptide is highly structured in the absence of IGF-1, and peptides that preorganize the binding elements were selected during the sorting.

About this Structure

1LB7 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.

Reference

Rapid identification of small binding motifs with high-throughput phage display: discovery of peptidic antagonists of IGF-1 function., Deshayes K, Schaffer ML, Skelton NJ, Nakamura GR, Kadkhodayan S, Sidhu SS, Chem Biol. 2002 Apr;9(4):495-505. PMID:11983338

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