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3t7a

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3t7a]] 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=3T7A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T7A FirstGlance]. <br>
<table><tr><td colspan='2'>[[3t7a]] 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=3T7A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T7A FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3t54|3t54]], [[3t99|3t99]], [[3t9a|3t9a]], [[3t9b|3t9b]], [[3t9c|3t9c]], [[3t9d|3t9d]], [[3t9e|3t9e]], [[3t9f|3t9f]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3t54|3t54]], [[3t99|3t99]], [[3t9a|3t9a]], [[3t9b|3t9b]], [[3t9c|3t9c]], [[3t9d|3t9d]], [[3t9e|3t9e]], [[3t9f|3t9f]]</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPIP5K2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPIP5K2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Diphosphoinositol-pentakisphosphate_kinase Diphosphoinositol-pentakisphosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.24 2.7.4.24] </span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Diphosphoinositol-pentakisphosphate_kinase Diphosphoinositol-pentakisphosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.24 2.7.4.24] </span></td></tr>
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<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=3t7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t7a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t7a RCSB], [http://www.ebi.ac.uk/pdbsum/3t7a PDBsum]</span></td></tr>
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<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=3t7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t7a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t7a RCSB], [http://www.ebi.ac.uk/pdbsum/3t7a PDBsum]</span></td></tr>
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<table>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/VIP2_HUMAN VIP2_HUMAN]] Bifunctional inositol kinase that acts in concert with the IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, exocytosis, insulin signaling and neutrophil activation. Phosphorylates inositol hexakisphosphate (InsP6) at positions 1 or 3 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates at position 1 or 3 PP-InsP5, produced by IP6Ks from InsP6, to produce (PP)2-InsP4.<ref>PMID:17690096</ref> <ref>PMID:17702752</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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Structural basis for an inositol pyrophosphate kinase surmounting phosphate crowding.,Wang H, Falck JR, Hall TM, Shears SB Nat Chem Biol. 2011 Nov 27. doi: 10.1038/nchembio.733. PMID:22119861<ref>PMID:22119861</ref>
Structural basis for an inositol pyrophosphate kinase surmounting phosphate crowding.,Wang H, Falck JR, Hall TM, Shears SB Nat Chem Biol. 2011 Nov 27. doi: 10.1038/nchembio.733. PMID:22119861<ref>PMID:22119861</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
== References ==
== References ==
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[[Category: Diphosphoinositol-pentakisphosphate kinase]]
[[Category: Diphosphoinositol-pentakisphosphate kinase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Falck, J.]]
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[[Category: Falck, J]]
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[[Category: Hall, T M.T.]]
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[[Category: Hall, T M.T]]
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[[Category: Shears, S B.]]
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[[Category: Shears, S B]]
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[[Category: Wang, H.]]
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[[Category: Wang, H]]
[[Category: Atp-grasp fold]]
[[Category: Atp-grasp fold]]
[[Category: Inositol pyrophosphate kinase]]
[[Category: Inositol pyrophosphate kinase]]
[[Category: Transferase]]
[[Category: Transferase]]

Revision as of 10:21, 25 December 2014

Crystal structure of the catalytic domain of human diphosphoinositol pentakisphosphate kinase 2 (PPIP5K2) in complex with ADP at pH 5.2

3t7a, resolution 1.70Å

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