Dissecting the Structural Dynamics of Authentic Cholesteryl Ester Transfer Protein for the Discovery of Potential Lead Compounds: A Theoretical Study.

ABSTRACT: Current structural and functional investigations of cholesteryl ester transfer protein (CETP) inhibitor design are nearly entirely based on a fully active mutation (CETP^Mutant) constructed for protein crystallization, limiting the study of the dynamic structural features of authentic CETP involved in lipid transport under physiological conditions. In this study, we conducted comprehensive molecular dynamics (MD) simulations of both authentic CETP (CETP^Authentic) and CETP^Mutant. Considering the structural differences between the N- and C-terminal domains of CETP^Authentic and CETP^Mutant, and their crucial roles in lipid transfer, we identified the two domains as binding pockets of the ligands for virtual screening to discover potential l

SUBMITTER: Zhao Y 

PROVIDER: S-EPMC10418423 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature