Exploring the potential of a structural alphabet-based tool for mining multiple target conformations and target flexibility insight.

ABSTRACT: Protein flexibility is often implied in binding with different partners and is essential for protein function. The growing number of macromolecular structures in the Protein Data Bank entries and their redundancy has become a major source of structural knowledge of the protein universe. The analysis of structural variability through available redundant structures of a target, called multiple target conformations (MTC), obtained using experimental or modeling methods and under different biological conditions or different sources is one way to explore protein flexibility. This analysis is essential to improve the understanding of various mechanisms associated with protein target function and flexibility. In this study, we explored structural variability of three biological targets by analyzi

SUBMITTER: Regad L 

PROVIDER: S-EPMC5560695 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature