Editorial: Protein recognition and associated diseases

Abstract

Protein-protein interactions are essential for many biological functions in all living organisms including cell signaling, molecular switching, transporters, receptors, and immunity. For the past few decades, tremendous advancements have been made in order to understand the recognition mechanism of protein-protein complex formation, reconstruct protein-protein interaction networks of an entire organism, and/or complete biochemical pathways. These efforts are mainly focussed on the identification of interacting proteins, prediction of binding site residues at their interface, evolutionary conservation of protein-protein complexes, prediction of protein-protein complex structures by docking, predicting the binding affinity of protein-protein complexes, and assessing the mutational effects on strength of binding and diseases (Gromiha, 2020). Recently, AlphaFold (Jumper et al., 2021) and its descendants (e.g., AlphaFoldMultimer, Evans et al., 2021), have demonstrated spectacular success in predicting structures of individual proteins and their complexes. Nevertheless, a significant number of cases and questions are still evading solutions and answers. This Research Topic on “Protein Recognition and Associated Diseases” addresses the recent advances in computational methodologies for the analysis and identification of important residues for binding, scoring, and ranking of structural models of protein-protein complexes, protein-protein interaction networks, and their applications in life sciences and human health.