1qw4

<table><tr><td colspan='2'>[[1qw4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QW4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1QW4 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3AR:N-OMEGA-PROPYL-L-ARGININE'>3AR</scene>, <scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitric-oxide_synthase_(NADPH_dependent) Nitric-oxide synthase (NADPH dependent)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1qw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qw4 OCA], [http://pdbe.org/1qw4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qw4 RCSB], [http://www.ebi.ac.uk/pdbsum/1qw4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qw4 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/NOS2_MOUSE NOS2_MOUSE]] Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such COX2.<ref>PMID:16373578</ref>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:12954642</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1qw4" style="background-color:#fffaf0;"></div>

[[Category: Lk3 transgenic mice]]

[[Category: Fedorov, R]]

[[Category: Ghosh, D K]]

[[Category: Hartmann, E]]

[[Category: Schlichting, I]]

[[Category: Oxidoreductase]]