2a7r

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{{Seed}}
 
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[[Image:2a7r.png|left|200px]]
 
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==Crystal structure of human Guanosine Monophosphate reductase 2 (GMPR2)==
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The line below this paragraph, containing "STRUCTURE_2a7r", creates the "Structure Box" on the page.
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<StructureSection load='2a7r' size='340' side='right'caption='[[2a7r]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2a7r]] is a 4 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=2A7R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A7R FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5GP:GUANOSINE-5-MONOPHOSPHATE'>5GP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_2a7r| PDB=2a7r | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2a7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a7r OCA], [https://pdbe.org/2a7r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a7r RCSB], [https://www.ebi.ac.uk/pdbsum/2a7r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a7r ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GMPR2_HUMAN GMPR2_HUMAN] Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. Plays a role in modulating cellular differentiation.<ref>PMID:12009299</ref> <ref>PMID:12669231</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a7/2a7r_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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/main_output.php?pdb_ID=2a7r ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Guanosine monophosphate reductase (GMPR) catalyzes the irreversible and NADPH-dependent reductive deamination of GMP to IMP, and plays a critical role in re-utilization of free intracellular bases and purine nucleosides. Here, we report the first crystal structure of human GMP reductase 2 (hGMPR2) in complex with GMP at 3.0 A resolution. The protein forms a tetramer composed of subunits adopting the ubiquitous (alpha/beta)8 barrel fold. Interestingly, the substrate GMP is bound to hGMPR2 through interactions with Met269, Ser270, Arg286, Ser288, and Gly290; this makes the conformation of the adjacent flexible binding region (residues 268-289) fixed, much like a door on a hinge. Structure comparison and sequence alignment analyses show that the conformation of the active site loop (residues 179-187) is similar to those of hGMPR1 and inosine monophosphate dehydrogenases (IMPDHs). We propose that Cys186 is the potential active site, and that the conformation of the loop (residues 129-133) suggests a preference for the coenzyme NADPH over NADH. This structure provides important information towards understanding the functions of members of the GMPR family.
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===Crystal structure of human Guanosine Monophosphate reductase 2 (GMPR2)===
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Crystal structure of human guanosine monophosphate reductase 2 (GMPR2) in complex with GMP.,Li J, Wei Z, Zheng M, Gu X, Deng Y, Qiu R, Chen F, Ji C, Gong W, Xie Y, Mao Y J Mol Biol. 2006 Feb 3;355(5):980-8. Epub 2005 Dec 1. PMID:16359702<ref>PMID:16359702</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16359702}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2a7r" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16359702 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16359702}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2A7R is a 4 chains structure of sequences 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=2A7R OCA].
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==Reference==
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<ref group="xtra">PMID:16359702</ref><references group="xtra"/>
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[[Category: GMP reductase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Chen, F.]]
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[[Category: Large Structures]]
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[[Category: Deng, Y.]]
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[[Category: Chen F]]
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[[Category: Gong, W.]]
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[[Category: Deng Y]]
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[[Category: Gu, X.]]
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[[Category: Gong W]]
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[[Category: Ji, C.]]
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[[Category: Gu X]]
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[[Category: Li, J.]]
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[[Category: Ji C]]
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[[Category: Mao, Y.]]
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[[Category: Li J]]
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[[Category: Qiu, R.]]
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[[Category: Mao Y]]
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[[Category: Wei, Z.]]
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[[Category: Qiu R]]
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[[Category: Xie, Y.]]
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[[Category: Wei Z]]
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[[Category: Zheng, M.]]
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[[Category: Xie Y]]
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[[Category: Oxidoreductase]]
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[[Category: Zheng M]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 11:23:10 2009''
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Current revision

Crystal structure of human Guanosine Monophosphate reductase 2 (GMPR2)

PDB ID 2a7r

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