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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=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2wm3]] is a 1 chain structure with sequence from [ | <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><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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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> | </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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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> | ||
</jmolCheckbox> | </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/ | </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> | <div style="clear:both"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Arrowsmith C]] | ||
[[Category: | [[Category: Bhatia C]] | ||
[[Category: | [[Category: Bountra C]] | ||
[[Category: Edwards | [[Category: Edwards A]] | ||
[[Category: Filippakopoulos | [[Category: Filippakopoulos P]] | ||
[[Category: Heightman | [[Category: Heightman T]] | ||
[[Category: Hozjan | [[Category: Hozjan V]] | ||
[[Category: Niesen | [[Category: Niesen F]] | ||
[[Category: Oppermann | [[Category: Oppermann U]] | ||
[[Category: Pilka | [[Category: Pilka E]] | ||
[[Category: Roos | [[Category: Roos AK]] | ||
[[Category: Savitsky | [[Category: Savitsky P]] | ||
[[Category: Ugochukwu | [[Category: Ugochukwu E]] | ||
[[Category: Weigelt | [[Category: Weigelt J]] | ||
[[Category: Yue | [[Category: Yue WW]] | ||
[[Category: | [[Category: Von Delft F]] | ||
Latest revision as of 13:14, 9 May 2024
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
FunctionNMRL1_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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