Structural Modeling of Wild and Mutant Forms of Human Plasma Platelet Activating Factor-Acetyl Hydrolase Enzyme.

ABSTRACT:

Purpose

To investigate the structural features of wild and mutant forms of the pPAF-AH enzyme that are responsible for coronary artery disease.

Methods

Mutant variants of human pPAF-AH having either V279F, Q281R, or both were modelled and evaluated for stereo chemical and structural correctness. The 3D coordinates of substrate PAF were retrieved from the PubChem database was solvated and minimized on Discovery Studio, and docked to the wild and mutant enzyme models. The top docked pose complex was refined by MD simulation.

Results

pPAF-AH model comprises of 420 amino acids in a α/β-hydrolase fold that contains a substrate-binding hydrophobic channel with an active site pocket having a catalytic triad of Ser273, Asp296 and His351. Mutations at positions 279 and 281 are

SUBMITTER: Khan MI 

PROVIDER: S-EPMC7751442 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature