Predicting the Effect of Mutations on Protein-Protein Binding Interactions through Structure-Based Interface Profiles.

ABSTRACT: The formation of protein-protein complexes is essential for proteins to perform their physiological functions in the cell. Mutations that prevent the proper formation of the correct complexes can have serious consequences for the associated cellular processes. Since experimental determination of protein-protein binding affinity remains difficult when performed on a large scale, computational methods for predicting the consequences of mutations on binding affinity are highly desirable. We show that a scoring function based on interface structure profiles collected from analogous protein-protein interactions in the PDB is a powerful predictor of protein binding affinity changes upon mutation. As a standalone feature, the differences between the interface profile score of the mutant and wild-

SUBMITTER: Brender JR 

PROVIDER: S-EPMC4624718 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature