1lb7
From Proteopedia
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
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 Page seeded by OCA on Fri May 2 23:44:46 2008
