Interplay of self-association and conformational flexibility in regulating protein function.

ABSTRACT: Many functional roles have been attributed to homodimers, the most common mode of protein self-association, notably in the regulation of enzymes, ion channels, transporters and transcription factors. Here we review findings that offer new insights into the different roles conformational flexibility plays in regulating homodimer function. Intertwined homodimers of two-domain proteins and their related family members display significant conformational flexibility, which translates into concerted motion between structural domains. This flexibility enables the corresponding proteins to regulate function across family members by modulating the spatial positions of key recognition surfaces of individual domains, to either maintain subunit interfaces, alter them or break them altogether, leading

SUBMITTER: Garton M 

PROVIDER: S-EPMC5941183 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature