2cbq
From Proteopedia
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[[Category: phage-display hapten binding]] | [[Category: phage-display hapten binding]] | ||
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Revision as of 14:59, 30 October 2007
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CRYSTAL STRUCTURE OF THE NEOCARZINOSTATIN 1TES15 MUTANT BOUND TO TESTOSTERONE HEMISUCCINATE.
Overview
We have recently applied in vitro evolution methods to create in, Neocarzinostatin a new binding site for a target molecule unrelated to its, natural ligand. The main objective of this work was to solve the structure, of some of the selected binders in complex with the target molecule:, testosterone. Three proteins (1a.15, 3.24 and 4.1) were chosen as, representative members of sequence families that came out of the selection, process within different randomization schemes. In order to evaluate, ligand-induced conformational adaptation, we also determined the structure, of one of the proteins (3.24) in the free and complexed forms., Surprisingly, all these mutants bind not one but two molecules of, testosterone in two very different ways. The 3.24 structure revealed that, the protein ... [(full description)]
About this Structure
2CBQ is a [Single protein] structure of sequence from [Streptomyces carzinostaticus] with SO4 and TH2 as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Structures of in vitro evolved binding sites on neocarzinostatin scaffold reveal unanticipated evolutionary pathways., Drevelle A, Graille M, Heyd B, Sorel I, Ulryck N, Pecorari F, Desmadril M, van Tilbeurgh H, Minard P, J Mol Biol. 2006 Apr 28;358(2):455-71. Epub 2006 Feb 20. PMID:16529771
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