Structure dictates the mechanism of ligand recognition in the histidine and maltose binding proteins.

ABSTRACT: Two mechanisms, induced fit (IF) and conformational selection (CS), have been proposed to explain ligand recognition coupled conformational changes. The histidine binding protein (HisJ) adopts the CS mechanism, in which a pre-equilibrium is established between the open and the closed states with the ligand binding to the closed state. Despite being structurally similar to HisJ, the maltose binding protein (MBP) adopts the IF mechanism, in which the ligand binds the open state and induces a transition to the closed state. To understand the molecular determinants of this difference, we performed molecular dynamics (MD) simulations of coarse-grained dual structure based models. We find that intra-protein contacts unique to the closed state are sufficient to promote the conformational transiti

SUBMITTER: Jayanthi LP 

PROVIDER: S-EPMC8244415 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature