1zvl

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Revision as of 08:34, 21 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1zvl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zvl, resolution 2.5Å" /> '''Rat Neuronal Nitric O...)
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File:1zvl.gif


1zvl, resolution 2.5Å

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Rat Neuronal Nitric Oxide Synthase Oxygenase Domain complexed with natural substrate L-Arg.

OverviewOverview

Nitric oxide synthesized from l-arginine by nitric oxide synthase isoforms, (NOS-I-III) is physiologically important but also can be deleterious when, overproduced. Selective NOS inhibitors are of clinical interest, given, their differing pathophysiological roles. Here we describe our approach to, target the unique NOS (6R,1'R,2'S)-5,6,7,8-tetrahydrobiopterin (H(4)Bip), binding site. By a combination of ligand- and structure-based design, the, structure-activity relationship (SAR) for a focused set of 41 pteridine, analogues on four scaffolds was developed, revealing selective NOS-I, inhibitors. The X-ray crystal structure of rat NOS-I dimeric-oxygenase, domain with H(4)Bip and l-arginine was determined and used for human, isoform homology modeling. All available NOS structural information was, subjected to comparative analysis of favorable protein-ligand interactions, using the GRID/concensus principal component analysis (CPCA) approach to, identify the isoform-specific interaction site. Our interpretation, based, on protein structures, is in good agreement with the ligand SAR and thus, permits the rational design of next-generation inhibitors targeting the, H(4)Bip binding site with enhanced isoform selectivity for therapeutics in, pathology with NO overproduction.

About this StructureAbout this Structure

1ZVL is a Single protein structure of sequence from Rattus norvegicus with ZN, HEM, H4B and ARG as ligands. Active as Nitric-oxide synthase, with EC number 1.14.13.39 Full crystallographic information is available from OCA.

ReferenceReference

Structural analysis of isoform-specific inhibitors targeting the tetrahydrobiopterin binding site of human nitric oxide synthases., Matter H, Kumar HS, Fedorov R, Frey A, Kotsonis P, Hartmann E, Frohlich LG, Reif A, Pfleiderer W, Scheurer P, Ghosh DK, Schlichting I, Schmidt HH, J Med Chem. 2005 Jul 28;48(15):4783-92. PMID:16033258

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