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==Crystal structure of NmrA-like family domain containing protein 1 in complex with niflumic acid== | ==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]] 1.85Å' scene=''> | <StructureSection load='2wm3' size='340' side='right' caption='[[2wm3]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2exx|2exx]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2exx|2exx]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wm3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wm3 OCA], [http://pdbe.org/2wm3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wm3 RCSB], [http://www.ebi.ac.uk/pdbsum/2wm3 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wm3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wm3 OCA], [http://pdbe.org/2wm3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wm3 RCSB], [http://www.ebi.ac.uk/pdbsum/2wm3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wm3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wm/2wm3_consurf.spt"</scriptWhenChecked> | <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> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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[[Category: Bhatia, C]] | [[Category: Bhatia, C]] | ||
[[Category: Bountra, C]] | [[Category: Bountra, C]] | ||
[[Category: Delft, F | [[Category: Delft, F von]] | ||
[[Category: Edwards, A]] | [[Category: Edwards, A]] | ||
[[Category: Filippakopoulos, P]] | [[Category: Filippakopoulos, P]] | ||
Revision as of 22:05, 24 January 2018
Crystal structure of NmrA-like family domain containing protein 1 in complex with niflumic acidCrystal structure of NmrA-like family domain containing protein 1 in complex with niflumic acid
Structural highlights
Function[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.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. References
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