What Strengthens Protein-Protein Interactions: Analysis and Applications of Residue Correlation Networks.

ABSTRACT: Identifying critical residues in protein-protein binding and efficiently designing stable and specific protein binders is challenging. In addition to direct contacts in a protein-protein binding interface, our study employs computation modeling to reveal the essential network of residue interaction and dihedral angle correlation critical in protein-protein recognition. We propose that mutating residues regions exhibited highly correlated motions within the interaction network can efficiently optimize protein-protein interactions to create tight and selective protein binders. We validated our strategy using ubiquitin (Ub) and MERS coronaviral papain-like protease (PLpro) complexes, where Ub is one central player in many cellular functions and PLpro is an antiviral drug target. Our designed

SUBMITTER: Hung TI 

PROVIDER: S-EPMC10055079 | biostudies-literature | 2023 Jun

REPOSITORIES: biostudies-literature