Decoupling a tandem-repeat protein: Impact of multiple loop insertions on a modular scaffold.

ABSTRACT: The simple topology and modular architecture of tandem-repeat proteins such as tetratricopeptide repeats (TPRs) and ankyrin repeats makes them straightforward to dissect and redesign. Repeat-protein stability can be manipulated in a predictable way using site-specific mutations. Here we explore a different type of modification - loop insertion - that will enable a simple route to functionalisation of this versatile scaffold. We previously showed that a single loop insertion has a dramatically different effect on stability depending on its location in the repeat array. Here we dissect this effect by a combination of multiple and alternated loop insertions to understand the origins of the context-dependent loss in stability. We find that the scaffold is remarkably robust in that its overall

SUBMITTER: Perez-Riba A 

PROVIDER: S-EPMC6817815 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature