Ontology highlight
ABSTRACT:
SUBMITTER: Lu S
PROVIDER: S-EPMC7734571 | biostudies-literature | 2015 Sep
REPOSITORIES: biostudies-literature
Lu Shaoyong S Deng Rong R Jiang Haiming H Song Huili H Li Shuai S Shen Qiancheng Q Huang Wenkang W Nussinov Ruth R Yu Jianxiu J Zhang Jian J
Structure (London, England : 1993) 20150806 9
Kinases use ATP to phosphorylate substrates; recent findings underscore the additional regulatory roles of ATP. Here, we propose a mechanism for allosteric regulation of Akt1 kinase phosphorylation by ATP. Our 4.7-μs molecular dynamics simulations of Akt1 and its mutants in the ATP/ADP bound/unbound states revealed that ATP occupancy of the ATP-binding site stabilizes the closed conformation, allosterically protecting pT308 by restraining phosphatase access and key interconnected residues on the ...[more]