Tunable Liaisons: eEF-2K, CaM, and Calcium.
In this issue of Structure, Lee et al. (2016) perform NMR analysis of calmodulin (CaM) binding to the eukaryotic elongation factor 2 kinase (eEF-2K). They find that eEF-2K interacts mainly with the C lobe of CaM in a Ca(2+)-tunable manner, revealing a high level of control in cellular homeostasis.
Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA; Department of Chemistry, University of Minnesota, Minneapolis, MN 55455, USA. Electronic address: vegli001@umn.edu.
Gianluigi
G
Veglia
Department of Chemistry, University of Minnesota, Minneapolis, MN 55455, USA.
Geoffrey
G
Li
D002118:Calcium; D010766:Phosphorylation; D011485:Protein Binding
D002118:Calcium