2wm3: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2wm3]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WM3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2wm3]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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><br>
</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><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><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://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://www.rcsb.org/pdb/explore.do?structureId=2wm3 RCSB], [http://www.ebi.ac.uk/pdbsum/2wm3 PDBsum]</span></td></tr>
<table>
</table>
== Function ==
[[http://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]]
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</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/chain_selection.php?pdb_ID=2ata ConSurf].
</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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Arrowsmith, C.]]
[[Category: Arrowsmith, C]]
[[Category: Bhatia, C.]]
[[Category: Bhatia, C]]
[[Category: Bountra, C.]]
[[Category: Bountra, C]]
[[Category: Delft, F Von.]]
[[Category: Delft, F Von]]
[[Category: Edwards, A.]]
[[Category: Edwards, A]]
[[Category: Filippakopoulos, P.]]
[[Category: Filippakopoulos, P]]
[[Category: Heightman, T.]]
[[Category: Heightman, T]]
[[Category: Hozjan, V.]]
[[Category: Hozjan, V]]
[[Category: Niesen, F.]]
[[Category: Niesen, F]]
[[Category: Oppermann, U.]]
[[Category: Oppermann, U]]
[[Category: Pilka, E.]]
[[Category: Pilka, E]]
[[Category: Roos, A K.]]
[[Category: Roos, A K]]
[[Category: Savitsky, P.]]
[[Category: Savitsky, P]]
[[Category: Ugochukwu, E.]]
[[Category: Ugochukwu, E]]
[[Category: Weigelt, J.]]
[[Category: Weigelt, J]]
[[Category: Yue, W W.]]
[[Category: Yue, W W]]
[[Category: Protein binding]]
[[Category: Protein binding]]

Revision as of 23:19, 24 December 2014

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

2wm3 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , ,
Resources:FirstGlance, OCA, RCSB, PDBsum

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

  1. ↑ Zhao Y, Zhang J, Li H, Li Y, Ren J, Luo M, Zheng X. An NADPH sensor protein (HSCARG) down-regulates nitric oxide synthesis by association with argininosuccinate synthetase and is essential for epithelial cell viability. J Biol Chem. 2008 Apr 18;283(16):11004-13. doi: 10.1074/jbc.M708697200. Epub 2008, Feb 8. PMID:18263583 doi:http://dx.doi.org/10.1074/jbc.M708697200
  2. ↑ Zheng X, Dai X, Zhao Y, Chen Q, Lu F, Yao D, Yu Q, Liu X, Zhang C, Gu X, Luo M. Restructuring of the dinucleotide-binding fold in an NADP(H) sensor protein. Proc Natl Acad Sci U S A. 2007 May 22;104(21):8809-14. Epub 2007 May 11. PMID:17496144
  3. ↑ Dai X, Li Y, Meng G, Yao S, Zhao Y, Yu Q, Zhang J, Luo M, Zheng X. NADPH is an allosteric regulator of HSCARG. J Mol Biol. 2009 Apr 17;387(5):1277-85. Epub 2009 Feb 28. PMID:19254724 doi:10.1016/j.jmb.2009.02.049

2wm3, resolution 1.85Å

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