Engineering the hCRBPII Domain-Swapped Dimer into a New Class of Protein Switches.

ABSTRACT: Protein conformational switches or allosteric proteins play a key role in the regulation of many essential biological pathways. Nonetheless, the implementation of protein conformational switches in protein design applications has proven challenging, with only a few known examples that are not derivatives of naturally occurring allosteric systems. We have discovered that the domain-swapped (DS) dimer of hCRBPII undergoes a large and robust conformational change upon retinal binding, making it a potentially powerful template for the design of protein conformational switches. Atomic resolution structures of the apo- and holo-forms illuminate a simple, mechanical movement involving sterically driven torsion angle flipping of two residues that drive the motion. We further demonstrate that the c

SUBMITTER: Ghanbarpour A 

PROVIDER: S-EPMC7358038 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature