1qw5
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(New page: 200px<br /><applet load="1qw5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qw5, resolution 2.7Å" /> '''Murine inducible nitr...)
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Revision as of 22:55, 20 November 2007
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Murine inducible nitric oxide synthase oxygenase domain in complex with W1400 inhibitor.
Overview
The high level of amino acid conservation and structural similarity in the, immediate vicinity of the substrate binding sites of the oxygenase domains, of the nitric-oxide synthase (NOS) isoforms (eNOSoxy, iNOSoxy, and, nNOSoxy) make the interpretation of the structural basis of inhibitor, isoform specificity a challenge and provide few clues for the design of, new selective compounds. Crystal structures of iNOSoxy and nNOSoxy, complexed with the inhibitors W1400 and Nomega-propyl-l-arginine provide a, rationale for their isoform specificity. It involves differences outside, the immediate active site as well as a conformational flexibility in the, active site that allows the adoption of distinct conformations in response, to interactions with the inhibitors. This flexibility is determined by, isoform-specific residues outside the active site.
About this Structure
1QW5 is a Single protein structure of sequence from Mus musculus with ZN, HEM, H4B and 14W as ligands. Active as Nitric-oxide synthase, with EC number 1.14.13.39 Full crystallographic information is available from OCA.
Reference
Structural basis for the specificity of the nitric-oxide synthase inhibitors W1400 and Nomega-propyl-L-Arg for the inducible and neuronal isoforms., Fedorov R, Hartmann E, Ghosh DK, Schlichting I, J Biol Chem. 2003 Nov 14;278(46):45818-25. Epub 2003 Sep 3. PMID:12954642
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