View source for 2wm3


==Crystal structure of NmrA-like family domain containing protein 1 in complex with niflumic acid==
<StructureSection load='2wm3' size='340' side='right'caption='[[2wm3]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2wm3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WM3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WM3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=NFL:2-{[3-(TRIFLUOROMETHYL)PHENYL]AMINO}NICOTINIC+ACID'>NFL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wm3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wm3 OCA], [https://pdbe.org/2wm3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wm3 RCSB], [https://www.ebi.ac.uk/pdbsum/2wm3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wm3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NMRL1_HUMAN NMRL1_HUMAN] Redox sensor protein. Undergoes restructuring and subcellular redistribution in response to changes in intracellular NADPH/NADP(+) levels. At low NADPH concentrations the protein is found mainly as a monomer, and binds argininosuccinate synthase (ASS1), the enzyme involved in nitric oxide synthesis. Association with ASS1 impairs its activity and reduces the production of nitric oxide, which subsecuently prevents apoptosis. Under normal NADPH concentrations, the protein is found as a dimer and hides the binding site for ASS1. The homodimer binds one molecule of NADPH. Has higher affinity for NADPH than for NADP(+). Binding to NADPH is necessary to form a stable dimer.<ref>PMID:18263583</ref> <ref>PMID:17496144</ref> <ref>PMID:19254724</ref> 
== 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/wm/2wm3_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=2wm3 ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Arrowsmith C]]
[[Category: Bhatia C]]
[[Category: Bountra C]]
[[Category: Edwards A]]
[[Category: Filippakopoulos P]]
[[Category: Heightman T]]
[[Category: Hozjan V]]
[[Category: Niesen F]]
[[Category: Oppermann U]]
[[Category: Pilka E]]
[[Category: Roos AK]]
[[Category: Savitsky P]]
[[Category: Ugochukwu E]]
[[Category: Weigelt J]]
[[Category: Yue WW]]
[[Category: Von Delft F]]