2gvg

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[[Image:2gvg.gif|left|200px]]
 
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{{Structure
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==Crystal Structure of human NMPRTase and its complex with NMN==
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|PDB= 2gvg |SIZE=350|CAPTION= <scene name='initialview01'>2gvg</scene>, resolution 2.2&Aring;
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<StructureSection load='2gvg' size='340' side='right'caption='[[2gvg]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=NMN:BETA-NICOTINAMIDE RIBOSE MONOPHOSPHATE'>NMN</scene>
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<table><tr><td colspan='2'>[[2gvg]] is a 6 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=2GVG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GVG FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Nicotinamide_phosphoribosyltransferase Nicotinamide phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.12 2.4.2.12]
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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]] 2.2&#8491;</td></tr>
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|GENE= NAMPT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NMN:BETA-NICOTINAMIDE+RIBOSE+MONOPHOSPHATE'>NMN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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}}
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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=2gvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gvg OCA], [https://pdbe.org/2gvg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gvg RCSB], [https://www.ebi.ac.uk/pdbsum/2gvg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gvg ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NAMPT_HUMAN NAMPT_HUMAN] Catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway (By similarity).
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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/gv/2gvg_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2gvg ConSurf].
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<div style="clear:both"></div>
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'''Crystal Structure of human NMPRTase and its complex with NMN'''
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==See Also==
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*[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Nicotinamide phosphoribosyltransferase (NMPRTase) has a crucial role in the salvage pathway of NAD+ biosynthesis, and a potent inhibitor of NMPRTase, FK866, can reduce cellular NAD+ levels and induce apoptosis in tumors. We have determined the crystal structures at up to 2.1-A resolution of human and murine NMPRTase, alone and in complex with the reaction product nicotinamide mononucleotide or the inhibitor FK866. The structures suggest that Asp219 is a determinant of substrate specificity of NMPRTase, which is confirmed by our mutagenesis studies. FK866 is bound in a tunnel at the interface of the NMPRTase dimer, and mutations in this binding site can abolish the inhibition by FK866. Contrary to current knowledge, the structures show that FK866 should compete directly with the nicotinamide substrate. Our structural and biochemical studies provide a starting point for the development of new anticancer agents.
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==About this Structure==
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2GVG is a [[Single protein]] structure of 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=2GVG OCA].
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==Reference==
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Molecular basis for the inhibition of human NMPRTase, a novel target for anticancer agents., Khan JA, Tao X, Tong L, Nat Struct Mol Biol. 2006 Jul;13(7):582-8. Epub 2006 Jun 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16783377 16783377]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Nicotinamide phosphoribosyltransferase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Khan JA]]
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[[Category: Khan, J A.]]
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[[Category: Tao X]]
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[[Category: Tao, X.]]
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[[Category: Tong L]]
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[[Category: Tong, L.]]
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[[Category: NMN]]
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[[Category: PO4]]
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[[Category: cancer]]
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[[Category: crystal]]
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[[Category: nmprtase]]
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[[Category: pbef]]
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[[Category: visfatin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:09:36 2008''
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Current revision

Crystal Structure of human NMPRTase and its complex with NMN

PDB ID 2gvg

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