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- W2945046717 abstract "Eukaryotic elongation factor 2 kinase (eEF-2K), an atypical calmodulin-activated protein kinase, regulates translational elongation by phosphorylating its substrate, eukaryotic elongation factor 2 (eEF-2), thereby reducing its affinity for the ribosome. The activation and activity of eEF-2K are critical for survival under energy-deprived conditions and is implicated in a variety of essential physiological processes. Previous biochemical experiments have indicated that the binding site for the substrate eEF-2 is located in the C-terminal domain of eEF-2K, a region predicted to harbor several α-helical repeats. Here, using NMR methodology, we have determined the solution structure of a C-terminal fragment of eEF-2K, eEF-2K562-725 that encodes two α-helical repeats. The structure of eEF-2K562-725 shows signatures characteristic of TPR domains and of their SEL1-like sub-family. Furthermore, using the analyses of NMR spectral perturbations and ITC measurements, we have localized the eEF-2 binding site on eEF-2K562-725. We find that eEF-2K562-725 engages eEF-2 with an affinity comparable to that of the full-length enzyme. Furthermore, eEF-2K562-725 is able to inhibit the phosphorylation of eEF-2 by full-length eEF-2K in trans. Our present studies establish that eEF-2K562-725 encodes the major elements necessary to enable the eEF-2K/eEF-2 interactions." @default.
- W2945046717 created "2019-05-29" @default.
- W2945046717 creator A5037679799 @default.
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- W2945046717 date "2019-07-01" @default.
- W2945046717 modified "2023-10-14" @default.
- W2945046717 title "Solution Structure of the Carboxy-Terminal Tandem Repeat Domain of Eukaryotic Elongation Factor 2 Kinase and Its Role in Substrate Recognition" @default.
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- W2945046717 doi "https://doi.org/10.1016/j.jmb.2019.05.019" @default.
- W2945046717 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6599559" @default.
- W2945046717 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31108082" @default.
- W2945046717 hasPublicationYear "2019" @default.
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