Structural Consequences of Multisite Phosphorylation in the BAK1 Kinase Domain.

ABSTRACT: Multisite phosphorylation is an important mechanism of post-translational control of protein kinases. The effects of combinations of possible phosphorylation states on protein kinase activity are difficult to study experimentally because of challenges in isolating a particular phosphorylation state; surprising little effort on this topic has been expended in computational studies. To understand the effects of multisite phosphorylation on the plant protein kinase brassinosteroid insensitive 1-associated kinase 1 (BAK1) conformational ensemble, we performed Gaussian accelerated molecular dynamics simulations on eight BAK1 mod-forms involving phosphorylation of the four activation-loop threonine residues and binding of ATP-Mg²⁺. We find that unphosphorylated BAK1 transitions into a

SUBMITTER: Moffett AS 

PROVIDER: S-EPMC7002984 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature