1qw6
Rat neuronal nitric oxide synthase oxygenase domain in complex with N-omega-propyl-L-Arg.
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OverviewOverview
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 StructureAbout this Structure
1QW6 is a Single protein structure of sequence from Rattus norvegicus with ZN, HEM, H4B and 3AR as ligands. Active as Nitric-oxide synthase, with EC number 1.14.13.39 Full crystallographic information is available from OCA.
ReferenceReference
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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