5y9m
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of CK2a2 form 3== | |
| + | <StructureSection load='5y9m' size='340' side='right' caption='[[5y9m]], [[Resolution|resolution]] 2.01Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5y9m]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y9M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y9M FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NIO:NICOTINIC+ACID'>NIO</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/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 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=5y9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y9m OCA], [http://pdbe.org/5y9m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y9m RCSB], [http://www.ebi.ac.uk/pdbsum/5y9m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y9m ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/CSK22_HUMAN CSK22_HUMAN]] Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.<ref>PMID:11239457</ref> <ref>PMID:11704824</ref> <ref>PMID:16193064</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The catalytic subunits of protein kinase CK2 are classified into two subtypes: CK2alpha1 and CK2alpha2. CK2alpha1 is an attractive drug-discovery target for various diseases such as cancers and nephritis. CK2alpha2 is defined as an off-target of CK2alpha1 and is a potential target in the development of male contraceptive drugs. High-resolution crystal structures of both isozymes are likely to provide crucial clues for the design of selective inhibitors of CK2alpha1 and/or CK2alpha2. To date, several crystal structures of CK2alpha1 have been solved at high resolutions of beyond 1.5 A. However, crystal structures of CK2alpha2 have barely achieved a low resolution of around 3 A because of the formation of needle-shaped crystals. In this study, new crystal forms were exploited and one provided a crystal structure of CK2alpha2 at 1.89 A resolution. This result, together with the structure of CK2alpha1, will assist in the development of highly selective inhibitors for both isozymes. | ||
| - | + | Crystal structures of human CK2alpha2 in new crystal forms arising from a subtle difference in salt concentration.,Tsuyuguchi M, Nakaniwa T, Kinoshita T Acta Crystallogr F Struct Biol Commun. 2018 May 1;74(Pt 5):288-293. doi:, 10.1107/S2053230X18005204. Epub 2018 Apr 16. PMID:29717996<ref>PMID:29717996</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5y9m" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Non-specific serine/threonine protein kinase]] | ||
[[Category: Kinoshita, T]] | [[Category: Kinoshita, T]] | ||
[[Category: Tsuyuguchi, M]] | [[Category: Tsuyuguchi, M]] | ||
| + | [[Category: Protein kinase]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 05:26, 16 May 2018
Crystal structure of CK2a2 form 3
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