1LB7
IGF-F1-1, A PEPTIDE ANTAGONIST OF IGF-1
Summary for 1LB7
| Entry DOI | 10.2210/pdb1lb7/pdb |
| Descriptor | IGF-1 ANTAGONIST F1-1 (1 entity in total) |
| Functional Keywords | loop-helix, disulfide, de novo protein |
| Total number of polymer chains | 1 |
| Total formula weight | 1879.22 |
| Authors | Deshayes, K.,Schaffer, M.L.,Skelton, N.J.,Nakamura, G.R.,Kadkhodayan, S.,Sidhu, S.S. (deposition date: 2002-04-02, release date: 2002-06-19, Last modification date: 2024-10-30) |
| Primary citation | Deshayes, K.,Schaffer, M.L.,Skelton, N.J.,Nakamura, G.R.,Kadkhodayan, S.,Sidhu, S.S. Rapid identification of small binding motifs with high-throughput phage display: discovery of peptidic antagonists of IGF-1 function. Chem.Biol., 9:495-505, 2002 Cited by PubMed Abstract: A panel of 22 naïve 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. PubMed: 11983338DOI: 10.1016/S1074-5521(02)00129-1 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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