4hok
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4hok]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HOK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HOK FirstGlance]. <br> | <table><tr><td colspan='2'>[[4hok]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HOK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HOK FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.77Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4hok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hok OCA], [https://pdbe.org/4hok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hok RCSB], [https://www.ebi.ac.uk/pdbsum/4hok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hok ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4hok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hok OCA], [https://pdbe.org/4hok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hok RCSB], [https://www.ebi.ac.uk/pdbsum/4hok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hok ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/KC1E_HUMAN KC1E_HUMAN] Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates DVL1. Central component of the circadian clock. In balance with PP1, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phospohorylation. Controls PER1 and PER2 nuclear transport and degradation. Inhibits cytokine-induced granuloytic differentiation.<ref>PMID:12556519</ref> <ref>PMID:15070676</ref> <ref>PMID:15917222</ref> <ref>PMID:16790549</ref> | [https://www.uniprot.org/uniprot/KC1E_HUMAN KC1E_HUMAN] Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates DVL1. Central component of the circadian clock. In balance with PP1, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phospohorylation. Controls PER1 and PER2 nuclear transport and degradation. Inhibits cytokine-induced granuloytic differentiation.<ref>PMID:12556519</ref> <ref>PMID:15070676</ref> <ref>PMID:15917222</ref> <ref>PMID:16790549</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Casein kinase 1 epsilon (CK1epsilon) and its closest homologue CK1delta are key regulators of diverse cellular processes. We report two crystal structures of PF4800567, a potent and selective inhibitor of CK1epsilon, bound to the kinase domains of human CK1epsilon and CK1delta as well as one apo CK1epsilon crystal structure. These structures provide a molecular basis for the strong and specific inhibitor interactions with CK1epsilon and suggest clues for further development of CK1delta inhibitors. | ||
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| - | Structural Basis for the Potent and Selective Inhibition of Casein Kinase 1 Epsilon.,Long AM, Zhao H, Huang X J Med Chem. 2012 Nov 9. PMID:23106386<ref>PMID:23106386</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4hok" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Current revision
crystal structure of apo ck1e
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