激酶
细胞生物学
延伸系数
GTP酶
生物
功能(生物学)
翻译(生物学)
磷酸化
机制(生物学)
真核翻译
计算生物学
核糖体
生物化学
物理
核糖核酸
基因
信使核糖核酸
量子力学
作者
Andrea Piserchio,Kevin N. Dalby,Ranajeet Ghose
标识
DOI:10.1016/j.tibs.2023.11.004
摘要
The α-kinase eukaryotic elongation factor 2 kinase (eEF-2K) regulates translational elongation by phosphorylating its ribosome-associated substrate, the GTPase eEF-2. eEF-2K is activated by calmodulin (CaM) through a distinctive mechanism unlike that in other CaM-dependent kinases (CAMK). We describe recent structural insights into this unique activation process and examine the effects of specific regulatory signals on this mechanism. We also highlight key unanswered questions to guide future structure-function studies. These include structural mechanisms which enable eEF-2K to interact with upstream/downstream partners and facilitate its integration of diverse inputs, including Ca
科研通智能强力驱动
Strongly Powered by AbleSci AI