1lb7
From Proteopedia
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| - | [[Image:1lb7.jpg|left|200px]] | + | [[Image:1lb7.jpg|left|200px]] |
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| - | '''IGF-F1-1, A PEPTIDE ANTAGONIST OF IGF-1''' | + | {{Structure |
| + | |PDB= 1lb7 |SIZE=350|CAPTION= <scene name='initialview01'>1lb7</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''IGF-F1-1, A PEPTIDE ANTAGONIST OF IGF-1''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LB7 is a [ | + | 1LB7 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LB7 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11983338 11983338] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Deshayes, K.]] | [[Category: Deshayes, K.]] | ||
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[[Category: peptide]] | [[Category: peptide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:28:52 2008'' |
Revision as of 10:28, 20 March 2008
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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 Mar 20 12:28:52 2008
