Folding cooperativity and allosteric function in the tandem-repeat protein class.

ABSTRACT: The term allostery was originally developed to describe structural changes in one binding site induced by the interaction of a partner molecule with a distant binding site, and it has been studied in depth in the field of enzymology. Here, we discuss the concept of action at a distance in relation to the folding and function of the solenoid class of tandem-repeat proteins such as tetratricopeptide repeats (TPRs) and ankyrin repeats. Distantly located repeats fold cooperatively, even though only nearest-neighbour interactions exist in these proteins. A number of repeat-protein scaffolds have been reported to display allosteric effects, transferred through the repeat array, that enable them to direct the activity of the multi-subunit enzymes within which they reside. We also highlight a rece

SUBMITTER: Perez-Riba A 

PROVIDER: S-EPMC5941182 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature