Mutational effects on protein–protein interactions

Abstract

Interatomically, protein’s ability to enact careful and tight interactions with its biomolecular partners is pivotal necessitating proper biological function. Protein–protein interactions (PPIs) are paramount in biological processes as manifested by their tenacious-cellular duties. Protein interfaces are the contact regions between proteins. The interface residues are under constant evolutionary restriction than surface residues. Variations in interface residues which alter binding affinity of proteins may lead to pronounce perturbation or absolute annulment of their functions, potentially resulting in diseases. Hence, wealth of investigations on mutational consequences of PPIs has evolved. The availability of both experimental and computational techniques to assess the effects of mutations on protein–protein binding affinities is essential for varieties of biomedical applications, spurring establishment of various mutational databases. Here, handy experimental and computational methods for detecting/predicting consequences of mutations on PPIs have been explored. Also, protocols and features of proteins utilized by these techniques have been elaborated and updates on mutational databases have been provided. Finally, case studies on mutations emerging at PPI interfaces and their involvements in human-related diseases such as cancer have been provided.