Rigid Residue Scan Simulations Systematically Reveal Residue Entropic Roles in Protein Allostery.

ABSTRACT: Intra-protein information is transmitted over distances via allosteric processes. This ubiquitous protein process allows for protein function changes due to ligand binding events. Understanding protein allostery is essential to understanding protein functions. In this study, allostery in the second PDZ domain (PDZ2) in the human PTP1E protein is examined as model system to advance a recently developed rigid residue scan method combining with configurational entropy calculation and principal component analysis. The contributions from individual residues to whole-protein dynamics and allostery were systematically assessed via rigid body simulations of both unbound and ligand-bound states of the protein. The entropic contributions of individual residues to whole-protein dynamics were evaluate

SUBMITTER: Kalescky R 

PROVIDER: S-EPMC4846164 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature