Tunable Liaisons: eEF-2K, CaM, and Calcium

Gianluigi Veglia; Geoffrey Li

doi:10.1016/j.str.2016.08.005

Tunable Liaisons: eEF-2K, CaM, and Calcium

Gianluigi Veglia
, Geoffrey Li

Structural Biology and Biophysics (TMED)

Research output: Contribution to journal › Short survey › peer-review

2 Scopus citations

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 Ca²⁺-tunable manner, revealing a high level of control in cellular homeostasis.

Original language	English (US)
Pages (from-to)	1438-1439
Number of pages	2
Journal	Structure
Volume	24
Issue number	9
DOIs	https://doi.org/10.1016/j.str.2016.08.005
State	Published - Sep 6 2016

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© 2016 Elsevier Ltd

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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 Ca2+-tunable manner, revealing a high level of control in cellular homeostasis.",

author = "Gianluigi Veglia and Geoffrey Li",

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AU - Li, Geoffrey

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AB - 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 Ca2+-tunable manner, revealing a high level of control in cellular homeostasis.

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UR - https://www.scopus.com/pages/publications/84985993709#tab=citedBy

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AN - SCOPUS:84985993709

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JO - Structure

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Tunable Liaisons: eEF-2K, CaM, and Calcium

Abstract

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