Considering Global and Local Conformational Changes in Molecular Docking - Abstract
Proteins undergo changes in their form (conformational changes) upon interaction with compounds/substrates. Molecular docking is an important tool used in the study of correlations between structure and function, aiding the understanding of several biological processes, shedding light on drug development. Structural rearrangements can occur during molecular recognition in order to optimize interactions in the complex, leading to local and global conformational changes. Conformational selection and induced fit are models that attempt to explain structural variation effects in molecular recognition. In this review we discuss the different strategies employed for global and local conformational changes, in both protein-ligand and protein-protein docking.