Ontology highlight
ABSTRACT:
SUBMITTER: Lee K
PROVIDER: S-EPMC5014583 | biostudies-literature | 2016 Sep
REPOSITORIES: biostudies-literature
Lee Kwangwoon K Alphonse Sébastien S Piserchio Andrea A Tavares Clint D J CD Giles David H DH Wellmann Rebecca M RM Dalby Kevin N KN Ghose Ranajeet R
Structure (London, England : 1993) 20160804 9
Binding of Ca(2+)-loaded calmodulin (CaM) activates eukaryotic elongation factor 2 kinase (eEF-2K) that phosphorylates eEF-2, its only known cellular target, leading to a decrease in global protein synthesis. Here, using an eEF-2K-derived peptide (eEF-2KCBD) that encodes the region necessary for its CaM-mediated activation, we provide a structural basis for their interaction. The striking feature of this association is the absence of Ca(2+) from the CaM C-lobe sites, even under high Ca(2+) condi ...[more]