Phosphorylation promotes binding affinity of Rap-Raf complex by allosteric modulation of switch loop dynamics.

ABSTRACT: The effects of phosphorylation of a serine residue on the structural and dynamic properties of Ras-like protein, Rap, and its interactions with effector protein Ras binding domain (RBD) of Raf kinase, in the presence of GTP, are investigated via molecular dynamics simulations. The simulations show that phosphorylation significantly effects the dynamics of functional loops of Rap which participate in the stability of the complex with effector proteins. The effects of phosphorylation on Rap are significant and detailed conformational analysis suggest that the Rap protein, when phosphorylated and with GTP ligand, samples different conformational space as compared to non-phosphorylated protein. In addition, phosphorylation of SER11 opens up a new cavity in the Rap protein which can be further

SUBMITTER: T D 

PROVIDER: S-EPMC6113251 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature