Disordered linkers in multidomain allosteric proteins: Entropic effect to favor the open state or enhanced local concentration to favor the closed state?

ABSTRACT: There are many multidomain allosteric proteins where an allosteric signal at the allosteric domain modifies the activity of the functional domain. Intrinsically disordered regions (linkers) are widely involved in this kind of regulation process, but the essential role they play therein is not well understood. Here, we investigated the effect of linkers in stabilizing the open or the closed states of multidomain proteins using combined thermodynamic deduction and coarse-grained molecular dynamics simulations. We revealed that the influence of linker can be fully characterized by an effective local concentration [B]₀ . When K_d is smaller than [B]₀ , the closed state would be favored; while the open state would be preferred when K_d is larger than [B

SUBMITTER: Li M 

PROVIDER: S-EPMC6194284 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature