Tunable Liaisons: eEF-2K, CaM, and Calcium
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Updated: Mar 15, 2026

Pull-down of Calmodulin-binding Proteins
Published on: January 23, 2012
Gianluigi Veglia1, Geoffrey Li2
1Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA; Department of Chemistry, University of Minnesota, Minneapolis, MN 55455, USA.
Abstract:
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.
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