1w8v
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(New page: 200px<br /> <applet load="1w8v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w8v, resolution 1.7Å" /> '''ENZYMATIC AND STRUCT...)
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Revision as of 17:41, 12 November 2007
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ENZYMATIC AND STRUCTURAL CHARACTERIZATION OF NON PEPTIDE LIGAND CYCLOPHILIN COMPLEXES
Overview
Piperidine ligands are described that provide the first examples of, non-peptidic ligand structures for the cyclophilin family of proteins., Crystal structures of two ligand complexes are compared with the, unliganded protein and show ligand-induced changes in side-chain, conformation and water binding. A peptidylprolyl cis-trans-isomerase assay, showed the dissociation constants of the two ligands to be 320 and 25 mM., This study also provides the first published data for both enzymatic, activity and three-dimensional structure for any protein-ligand complex, that binds with a high-millimolar dissociation constant. The structures, may be of relevance in the field of drug design, as they suggest starting, points for the design of larger tighter-binding analogues.
About this Structure
1W8V is a Single protein structure of sequence from Homo sapiens. Active as Peptidylprolyl isomerase, with EC number 5.2.1.8 Full crystallographic information is available from OCA.
Reference
Enzymatic and structural characterization of non-peptide ligand-cyclophilin complexes., Kontopidis G, Taylor P, Walkinshaw MD, Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):479-85. Epub 2004, Feb 25. PMID:14993672
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