A Molecular Dynamics Approach to Explore the Intramolecular Signal Transduction of PPAR-α.

ABSTRACT: Dynamics and functions of the peroxisome proliferator-activated receptor (PPAR)-α are modulated by the types of ligands that bind to the orthosteric sites. While several X-ray crystal structures of PPAR-α have been determined in their agonist-bound forms, detailed structural information in their apo and antagonist-bound states are still lacking. To address these limitations, we apply unbiased molecular dynamics simulations to three different PPAR-α systems to determine their modulatory mechanisms. Herein, we performed hydrogen bond and essential dynamics analyses to identify the important residues involved in polar interactions and conformational structural variations, respectively. Furthermore, betweenness centrality network analysis was carried out to identify key residues for intramolec

SUBMITTER: Basith S 

PROVIDER: S-EPMC6479491 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature