This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
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
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
Page seeded by OCA on Thu Feb 21 13:43:18 2008
