2ckp
From Proteopedia
(Difference between revisions)
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- | + | ==CRYSTAL STRUCTURE OF HUMAN CHOLINE KINASE ALPHA-2 IN COMPLEX WITH ADP== | |
- | [[ | + | <StructureSection load='2ckp' size='340' side='right' caption='[[2ckp]], [[Resolution|resolution]] 3.10Å' scene=''> |
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[2ckp]] is a 2 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=2CKP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CKP FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene><br> | ||
+ | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2cko|2cko]], [[2ckq|2ckq]]</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Choline_kinase Choline kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.32 2.7.1.32] </span></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=2ckp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ckp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ckp RCSB], [http://www.ebi.ac.uk/pdbsum/2ckp PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ck/2ckp_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </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="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Choline kinase, responsible for the phosphorylation of choline to phosphocholine as the first step of the CDP-choline pathway for the biosynthesis of phosphatidylcholine, has been recognized as a new target for anticancer therapy. Crystal structures of human choline kinase in its apo, ADP and phosphocholine-bound complexes, respectively, reveal the molecular details of the substrate binding sites. ATP binds in a cavity where residues from both the N and C-terminal lobes contribute to form a cleft, while the choline-binding site constitutes a deep hydrophobic groove in the C-terminal domain with a rim composed of negatively charged residues. Upon binding of choline, the enzyme undergoes conformational changes independently affecting the N-terminal domain and the ATP-binding loop. From this structural analysis and comparison with other kinases, and from mutagenesis data on the homologous Caenorhabditis elegans choline kinase, a model of the ternary ADP.phosphocholine complex was built that reveals the molecular basis for the phosphoryl transfer activity of this enzyme. | ||
- | + | Elucidation of human choline kinase crystal structures in complex with the products ADP or phosphocholine.,Malito E, Sekulic N, Too WC, Konrad M, Lavie A J Mol Biol. 2006 Nov 24;364(2):136-51. Epub 2006 Sep 3. PMID:17007874<ref>PMID:17007874</ref> | |
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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
+ | </div> | ||
- | + | ==See Also== | |
- | + | *[[Choline kinase|Choline kinase]] | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | + | ||
- | == | + | |
- | + | ||
- | + | ||
- | == | + | |
- | < | + | |
[[Category: Choline kinase]] | [[Category: Choline kinase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Lavie, A.]] | [[Category: Lavie, A.]] | ||
[[Category: Malito, E.]] | [[Category: Malito, E.]] | ||
- | [[Category: Alternative splicing]] | ||
[[Category: Choline kinase]] | [[Category: Choline kinase]] | ||
[[Category: Kinase]] | [[Category: Kinase]] | ||
[[Category: Phosphatydilcholine]] | [[Category: Phosphatydilcholine]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
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- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 18:19:44 2009'' |
Revision as of 05:28, 29 September 2014
CRYSTAL STRUCTURE OF HUMAN CHOLINE KINASE ALPHA-2 IN COMPLEX WITH ADP
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