1lb7: Difference between revisions
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==IGF-F1-1, A PEPTIDE ANTAGONIST OF IGF-1== | |||
<StructureSection load='1lb7' size='340' side='right'caption='[[1lb7]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1lb7]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LB7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LB7 FirstGlance]. <br> | |||
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lb7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lb7 OCA], [https://pdbe.org/1lb7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lb7 RCSB], [https://www.ebi.ac.uk/pdbsum/1lb7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lb7 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
== | |||
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. | 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. | ||
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<ref>PMID:11983338</ref> | |||
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 | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1lb7" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Deshayes K]] | |||
[[Category: Kadkhodayan S]] | |||
[[Category: Nakamura GR]] | |||
[[Category: Schaffer ML]] | |||
[[Category: Sidhu SS]] | |||
[[Category: Skelton NJ]] | |||