5j0a: Difference between revisions
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==Crystal structure of PDZ-binding kinase== | |||
<StructureSection load='5j0a' size='340' side='right' caption='[[5j0a]], [[Resolution|resolution]] 2.74Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5j0a]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J0A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J0A FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HC4:4-HYDROXYCINNAMIC+ACID'>HC4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mitogen-activated_protein_kinase_kinase Mitogen-activated protein kinase kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.12.2 2.7.12.2] </span></td></tr> | |||
<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=5j0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j0a OCA], [http://pdbe.org/5j0a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j0a RCSB], [http://www.ebi.ac.uk/pdbsum/5j0a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j0a ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/TOPK_HUMAN TOPK_HUMAN]] Phosphorylates MAP kinase p38. Seems to be active only in mitosis. May also play a role in the activation of lymphoid cells. When phosphorylated, forms a complex with TP53, leading to TP53 destabilization and attenuation of G2/M checkpoint during doxorubicin-induced DNA damage.<ref>PMID:10781613</ref> <ref>PMID:17482142</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The overexpression of PDZ-binding kinase/T-LAK cell-originated protein kinase (PBK/TOPK) has been associated with hematologic tumors, breast cancer and various other cancers. However, the three-dimensional structure of PBK has not been solved. In this study, we determined the crystal structure of human PBK, which has two phospho-mimicking mutations T9E and T198E. The structural data indicated that PBK may assemble into an inactive dimer in alkaline conditions. Analytical size-exclusion chromatography and analytical ultracentrifugation confirmed that PBK exists in a conformational transition between dimers and monomers at different pH conditions. Co-IP and kinase assays suggested that the active state of PBK is a monomer and does not form a dimer even under alkaline conditions. These results showed that the conformational transition of PBK is important for its kinase activity regulation. Collectively, our observations may provide a novel starting point for structure-based functional studies. | |||
The crystal structure of an inactive dimer of PDZ-binding kinase.,Dong C, Tang X, Xie Y, Zou Q, Yang X, Zhou H Biochem Biophys Res Commun. 2016 Aug 5;476(4):586-93. doi:, 10.1016/j.bbrc.2016.05.166. Epub 2016 Jun 1. PMID:27262437<ref>PMID:27262437</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5j0a" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Mitogen-activated protein kinase kinase]] | |||
[[Category: Yang, X]] | |||
[[Category: Zhou, H]] | |||
[[Category: Zou, Q W]] | |||
[[Category: Protein kinase]] | |||
[[Category: Transferase]] | |||
Revision as of 21:08, 10 September 2016
Crystal structure of PDZ-binding kinase
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