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Sci. Signal., 2 March 2010
Vol. 3, Issue 111, p. ra17
[DOI: 10.1126/scisignal.2000525]


Editor's Summary

In the Loop
Conventional serine-threonine protein kinases constitute a huge family of enzymes that regulate many processes in the cell. In contrast, the family of {alpha}-kinases is far smaller and consists of atypical kinases that regulate a much more restricted range of functions. Ye et al. have now solved the crystal structure of a prototypical member of the {alpha}-kinase family and identified features of the active site of these enzymes that may account for their different activities relative to those of the conventional kinases. Ye et al. solved the crystal structures of the catalytic domain of Dictyostelium myosin II heavy chain kinase A (MHCK A) bound to various nucleotides and compared them to structures of the kinase domains of TRPM7, another {alpha}-kinase, and PKA, a conventional protein kinase. In addition to demonstrating that MHCK A and TRPM7 share an almost identical core catalytic domain, solving these structures has identified critical features that distinguish the {alpha}-kinases from the conventional protein kinases. In particular, the authors identified a metal ion-binding loop that regulates access to the active site and an aspartylphosphate residue that may act as an intermediate in the phosphorylation of substrates.

Citation: Q. Ye, S. W. Crawley, Y. Yang, G. P. Côté, Z. Jia, Crystal Structure of the {alpha}-Kinase Domain of Dictyostelium Myosin Heavy Chain Kinase A. Sci. Signal. 3, ra17 (2010).

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Autophosphorylation Activates Dictyostelium Myosin II Heavy Chain Kinase A by Providing a Ligand for an Allosteric Binding Site in the {alpha}-Kinase Domain.
S. W. Crawley, M. S. Gharaei, Q. Ye, Y. Yang, B. Raveh, N. London, O. Schueler-Furman, Z. Jia, and G. P. Cote (2011)
J. Biol. Chem. 286, 2607-2616
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