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4bxb
From Proteopedia
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| - | ''' | + | ==Monoclinic Complex Structure of Protein Kinase CK2 Catalytic Subunit with a Benzotriazole-Based Inhibitor Generated by click-chemistry== |
| + | <StructureSection load='4bxb' size='340' side='right' caption='[[4bxb]], [[Resolution|resolution]] 2.35Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4bxb]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BXB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BXB FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=JRJ:4-[4-[2-[4,5,6,7-TETRAKIS(BROMANYL)BENZOTRIAZOL-2-YL]ETHYL]-1,2,3-TRIAZOL-1-YL]BUTAN-1-AMINE'>JRJ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bxa|4bxa]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=4bxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bxb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bxb RCSB], [http://www.ebi.ac.uk/pdbsum/4bxb PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | New 4,5,6,7-tetrabromo benzotriazole derivatives have been synthesized, and their activities against CK2 have been tested. A click chemistry approach based on the copper-catalyzed azide-alkyne cycloaddition has been utilized to connect benzotriazoles, which efficiently interact with the ATP-binding site, to other subunits designed to simultaneously bind to the active and the substrate-binding sites of the enzyme. Docking studies allowed us to identify key interactions between CK2 and the designed ligands, which will be useful to optimize this series of multisite-directed inhibitors. | ||
| - | + | Multisite-directed inhibitors of protein kinase CK2: new challenges.,Swider R, Maslyk M, Martin-Santamaria S, Ramos A, de Pascual-Teresa B Mol Cell Biochem. 2011 Oct;356(1-2):117-9. doi: 10.1007/s11010-011-0962-7. Epub, 2011 Jul 13. PMID:21750979<ref>PMID:21750979</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Non-specific serine/threonine protein kinase]] | ||
| + | [[Category: Martin-Santamiaria, S.]] | ||
| + | [[Category: Maslyk, M.]] | ||
| + | [[Category: Niefind, K.]] | ||
| + | [[Category: Panchuk, R.]] | ||
| + | [[Category: Pascual-Teresa, B de.]] | ||
| + | [[Category: Ramos, A.]] | ||
| + | [[Category: Schnitzler, A.]] | ||
| + | [[Category: Skorokhyd, N.]] | ||
| + | [[Category: Swider, R.]] | ||
| + | [[Category: Atp-competitive inhibitor]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 07:33, 30 July 2014
Monoclinic Complex Structure of Protein Kinase CK2 Catalytic Subunit with a Benzotriazole-Based Inhibitor Generated by click-chemistry
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