4hgl
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4hgl]] is a 1 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=4HGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HGL FirstGlance]. <br> | <table><tr><td colspan='2'>[[4hgl]] is a 1 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=4HGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HGL FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0YO:2-[5-METHOXY-2-(QUINOLIN-3-YL)PYRIMIDIN-4-YL]-1,5,6,7-TETRAHYDRO-4H-PYRROLO[3,2-C]PYRIDIN-4-ONE'>0YO</scene>, <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]] 2.4Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0YO:2-[5-METHOXY-2-(QUINOLIN-3-YL)PYRIMIDIN-4-YL]-1,5,6,7-TETRAHYDRO-4H-PYRROLO[3,2-C]PYRIDIN-4-ONE'>0YO</scene>, <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=4hgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hgl OCA], [https://pdbe.org/4hgl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hgl RCSB], [https://www.ebi.ac.uk/pdbsum/4hgl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hgl 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=4hgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hgl OCA], [https://pdbe.org/4hgl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hgl RCSB], [https://www.ebi.ac.uk/pdbsum/4hgl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hgl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/KC1G3_HUMAN KC1G3_HUMAN] Serine/threonine-protein kinase. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Regulates fast synaptic transmission mediated by glutamate (By similarity). | [https://www.uniprot.org/uniprot/KC1G3_HUMAN KC1G3_HUMAN] Serine/threonine-protein kinase. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Regulates fast synaptic transmission mediated by glutamate (By similarity). | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Aberrant activation of the Wnt pathway is believed to drive the development and growth of some cancers. The central role of CK1gamma in Wnt signal transduction makes it an attractive target for the treatment of Wnt-pathway dependent cancers. We describe a structure-based approach that led to the discovery of a series of pyridyl pyrrolopyridinones as potent and selective CK1gamma inhibitors. These compounds exhibited good enzyme and cell potency, as well as selectivity against other CK1 isoforms. A single oral dose of compound 13 resulted in significant inhibition of LRP6 phosphorylation in a mouse tumor PD model. | ||
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| - | Structure-Based Design of Potent and Selective CK1gamma Inhibitors.,Huang H, Acquaviva L, Berry V, Bregman H, Chakka N, O'Connor A, DiMauro EF, Dovey J, Epstein O, Grubinska B, Goldstein J, Gunaydin H, Hua Z, Huang X, Huang L, Human J, Long A, Newcomb J, Patel VF, Saffran D, Serafino R, Schneider S, Strathdee C, Tang J, Turci S, White R, Yu V, Zhao H, Wilson C, Martin MW ACS Med Chem Lett. 2012 Oct 18;3(12):1059-64. doi: 10.1021/ml300278f. eCollection, 2012 Dec 13. PMID:24900428<ref>PMID:24900428</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4hgl" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Casein kinase 3D structures|Casein kinase 3D structures]] | *[[Casein kinase 3D structures|Casein kinase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of ck1g3 with compound 1
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