Casein kinase

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== Structural highlights ==
== Structural highlights ==
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CK2 is a tetramer with a pair of 2 subunits – the α subunit is the catalytic one and the β subunit is the regulatory one. <scene name='46/468136/Cv/3'>CK1 inhibitors bind in the ATP binding pocket</scene>. <ref>PMID:22877629</ref> Water molecules are shown as red spheres.
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CK2 is a tetramer with a pair of 2 subunits – the α subunit is the catalytic one and the β subunit is the regulatory one. <scene name='46/468136/Cv/4'>CK1 inhibitors bind in the ATP binding pocket</scene>. <ref>PMID:22877629</ref> Water molecules are shown as red spheres.
</StructureSection>
</StructureSection>

Revision as of 12:56, 10 February 2019

Human casein kinase 1 γ3 complex with inhibitor (PDB code 4g16)

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3D Structures of casein kinase

Updated on 10-February-2019

References

  1. Eide EJ, Virshup DM. Casein kinase I: another cog in the circadian clockworks. Chronobiol Int. 2001 May;18(3):389-98. PMID:11475410
  2. Pinna LA, Meggio F. Protein kinase CK2 ("casein kinase-2") and its implication in cell division and proliferation. Prog Cell Cycle Res. 1997;3:77-97. PMID:9552408
  3. Hua Z, Huang X, Bregman H, Chakka N, DiMauro EF, Doherty EM, Goldstein J, Gunaydin H, Huang H, Mercede S, Newcomb J, Patel VF, Turci SM, Yan J, Wilson C, Martin MW. 2-Phenylamino-6-cyano-1H-benzimidazole-based isoform selective casein kinase 1 gamma (CK1gamma) inhibitors. Bioorg Med Chem Lett. 2012 Sep 1;22(17):5392-5. doi: 10.1016/j.bmcl.2012.07.046. , Epub 2012 Jul 20. PMID:22877629 doi:10.1016/j.bmcl.2012.07.046

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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