Enhancing response of a protein conformational switch by using two disordered ligand binding domains.

ABSTRACT: Introduction: Protein conformational switches are often constructed by fusing an input domain, which recognizes a target ligand, to an output domain that establishes a biological response. Prior designs have employed binding-induced folding of the input domain to drive a conformational change in the output domain. Adding a second input domain can in principle harvest additional binding energy for performing useful work. It is not obvious, however, how to fuse two binding domains to a single output domain such that folding of both binding domains combine to effect conformational change in the output domain. Methods: Here, we converted the ribonuclease barnase (Bn) to a switchable enzyme by duplicating a C-terminal portion of its sequence and appending it to its N-terminus, the

SUBMITTER: Sekhon H 

PROVIDER: S-EPMC10018487 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature