| Literature DB >> 25963826 |
Bertrand Simon1, Anne-Sophie Huart1, Matthias Wilmanns2.
Abstract
Many human protein kinases are regulated by the calcium-sensor protein calmodulin, which binds to a short flexible segment C-terminal to the enzyme's catalytic kinase domain. Our understanding of the molecular mechanism of kinase activity regulation by calcium/calmodulin has been advanced by the structures of two protein kinases-calmodulin kinase II and death-associated protein kinase 1-bound to calcium/calmodulin. Comparison of these two structures reveals a surprising level of diversity in the overall kinase-calcium/calmodulin arrangement and functional readout of activity, as well as complementary mechanisms of kinase regulation such as phosphorylation.Entities:
Keywords: Autoinhibitory and calmodulin-binding domains; Autoregulatory domain; Calcium/calmodulin-dependent protein kinase crystal structure comparison; Death-associated protein kinase; Phosphorylation
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Year: 2015 PMID： 25963826 DOI： 10.1016/j.bmc.2015.04.051
Source DB: PubMed Journal: Bioorg Med Chem ISSN： 0968-0896 Impact factor: 3.641