1qw6: Difference between revisions

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-[[Image:1qw6.jpg|left|200px]]
-<!--
+==Rat neuronal nitric oxide synthase oxygenase domain in complex with N-omega-propyl-L-Arg.==
-The line below this paragraph, containing "STRUCTURE_1qw6", creates the "Structure Box" on the page.
+<StructureSection load='1qw6' size='340' side='right'caption='[[1qw6]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1qw6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QW6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QW6 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</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>
-{{STRUCTURE_1qw6|  PDB=1qw6  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qw6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qw6 OCA], [https://pdbe.org/1qw6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qw6 RCSB], [https://www.ebi.ac.uk/pdbsum/1qw6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qw6 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/NOS1_RAT NOS1_RAT] Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Inhibitory transmitter for non-adrenergic and non-cholinergic nerves in the colorectum. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR. Inhibitory transmitter for non-adrenergic and non-cholinergic nerves in the colorectum.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qw/1qw6_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qw6 ConSurf].
+<div style="clear:both"></div>
-'''Rat neuronal nitric oxide synthase oxygenase domain in complex with N-omega-propyl-L-Arg.'''
+==See Also==
+*[[Nitric Oxide Synthase 3D structures|Nitric Oxide Synthase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-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.
+[[Category: Large Structures]]
-==About this Structure==
-QW6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QW6 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:[http://www.ncbi.nlm.nih.gov/pubmed/12954642 12954642]
-[[Category: Nitric-oxide synthase]]
 [[Category: Rattus norvegicus]]
-[[Category: Single protein]]
+[[Category: Fedorov R]]
-[[Category: Fedorov, R.]]
+[[Category: Ghosh DK]]
-[[Category: Ghosh, D K.]]
+[[Category: Hartmann E]]
-[[Category: Hartmann, E.]]
+[[Category: Schlichting I]]
-[[Category: Schlichting, I.]]
-[[Category: Rat nnosoxy complex with n-omega-propyl-l-arg]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:46:07 2008''