Conformational energy range of ligands in protein crystal structures: The difficult quest for accurate understanding.

ABSTRACT: In this review, we address a fundamental question: What is the range of conformational energies seen in ligands in protein-ligand crystal structures? This value is important biophysically, for better understanding the protein-ligand binding process; and practically, for providing a parameter to be used in many computational drug design methods such as docking and pharmacophore searches. We synthesize a selection of previously reported conflicting results from computational studies of this issue and conclude that high ligand conformational energies really are present in some crystal structures. The main source of disagreement between different analyses appears to be due to divergent treatments of electrostatics and solvation. At the same time, however, for many ligands, a high conformationa

SUBMITTER: Peach ML 

PROVIDER: S-EPMC5553890 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature