Intrinsic Disorder in Tetratricopeptide Repeat Proteins.

ABSTRACT: Among the realm of repeat containing proteins that commonly serve as "scaffolds" promoting protein-protein interactions, there is a family of proteins containing between 2 and 20 tetratricopeptide repeats (TPRs), which are functional motifs consisting of 34 amino acids. The most distinguishing feature of TPR domains is their ability to stack continuously one upon the other, with these stacked repeats being able to affect interaction with binding partners either sequentially or in combination. It is known that many repeat-containing proteins are characterized by high levels of intrinsic disorder, and that many protein tandem repeats can be intrinsically disordered. Furthermore, it seems that TPR-containing proteins share many characteristics with hybrid proteins containing ordered domains a

SUBMITTER: Van Bibber NW 

PROVIDER: S-EPMC7279152 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature