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1w2c

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[[Image:1w2c.jpg|left|200px]]<br /><applet load="1w2c" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1w2c, resolution 1.95&Aring;" />
 
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'''HUMAN INOSITOL (1,4,5) TRISPHOSPHATE 3-KINASE COMPLEXED WITH MN2+/AMPPNP/INS(1,4,5)P3'''<br />
 
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==Overview==
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==Human Inositol (1,4,5) trisphosphate 3-kinase complexed with Mn2+/AMPPNP/Ins(1,4,5)P3==
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Mammalian cells produce a variety of inositol phosphates (InsPs), including Ins(1,4,5)P3 that serves both as a second messenger and as a, substrate for inositol polyphosphate kinases (IPKs), which further, phosphorylate it. We report the structure of an IPK, the human, Ins(1,4,5)P3 3-kinase-A, both free and in complexes with substrates and, products. This enzyme catalyzes transfer of a phosphate from ATP to the, 3-OH of Ins(1,4,5)P3, and its X-ray crystal structure provides a template, for understanding a broad family of InsP kinases. The catalytic domain, consists of three lobes. The N and C lobes bind ATP and resemble protein, and lipid kinases, despite insignificant sequence similarity. The third, lobe binds inositol phosphate and is a unique four-helix insertion in the, C lobe. This lobe embraces all of the phosphates of Ins(1,4,5)P3 in a, positively charged pocket, explaining the enzyme's substrate specificity, and its inability to phosphorylate PtdIns(4,5)P2, the membrane-resident, analog of Ins(1,4,5)P3.
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<StructureSection load='1w2c' size='340' side='right'caption='[[1w2c]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1w2c]] is a 2 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=1W2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W2C FirstGlance]. <br>
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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]] 1.95&#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=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=I3P:D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE'>I3P</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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=1w2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w2c OCA], [https://pdbe.org/1w2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w2c RCSB], [https://www.ebi.ac.uk/pdbsum/1w2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w2c ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/IP3KA_HUMAN IP3KA_HUMAN]
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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/w2/1w2c_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=1w2c 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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Mammalian cells produce a variety of inositol phosphates (InsPs), including Ins(1,4,5)P3 that serves both as a second messenger and as a substrate for inositol polyphosphate kinases (IPKs), which further phosphorylate it. We report the structure of an IPK, the human Ins(1,4,5)P3 3-kinase-A, both free and in complexes with substrates and products. This enzyme catalyzes transfer of a phosphate from ATP to the 3-OH of Ins(1,4,5)P3, and its X-ray crystal structure provides a template for understanding a broad family of InsP kinases. The catalytic domain consists of three lobes. The N and C lobes bind ATP and resemble protein and lipid kinases, despite insignificant sequence similarity. The third lobe binds inositol phosphate and is a unique four-helix insertion in the C lobe. This lobe embraces all of the phosphates of Ins(1,4,5)P3 in a positively charged pocket, explaining the enzyme's substrate specificity and its inability to phosphorylate PtdIns(4,5)P2, the membrane-resident analog of Ins(1,4,5)P3.
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==About this Structure==
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Structure of a human inositol 1,4,5-trisphosphate 3-kinase: substrate binding reveals why it is not a phosphoinositide 3-kinase.,Gonzalez B, Schell MJ, Letcher AJ, Veprintsev DB, Irvine RF, Williams RL Mol Cell. 2004 Sep 10;15(5):689-701. PMID:15350214<ref>PMID:15350214</ref>
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1W2C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ANP:'>ANP</scene> and <scene name='pdbligand=I3P:'>I3P</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.7.127 2.1.7.127] Known structural/functional Site: <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W2C OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure of a human inositol 1,4,5-trisphosphate 3-kinase: substrate binding reveals why it is not a phosphoinositide 3-kinase., Gonzalez B, Schell MJ, Letcher AJ, Veprintsev DB, Irvine RF, Williams RL, Mol Cell. 2004 Sep 10;15(5):689-701. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15350214 15350214]
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</div>
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<div class="pdbe-citations 1w2c" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Transferase]]
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[[Category: Gonzalez B]]
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[[Category: Gonzalez, B.]]
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[[Category: Irvine RF]]
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[[Category: Irvine, R.F.]]
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[[Category: Schell MJ]]
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[[Category: Schell, M.J.]]
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[[Category: Williams RL]]
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[[Category: Williams, R.L.]]
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[[Category: ANP]]
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[[Category: I3P]]
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[[Category: MN]]
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[[Category: SO4]]
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[[Category: amppnp]]
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[[Category: inositol phosphate kinase]]
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[[Category: ip3]]
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[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:18:25 2008''
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Current revision

Human Inositol (1,4,5) trisphosphate 3-kinase complexed with Mn2+/AMPPNP/Ins(1,4,5)P3

PDB ID 1w2c

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