Ligand-induced conformational switch in an artificial bidomain protein scaffold.

ABSTRACT: Artificial proteins binding any predefined "target" protein can now be efficiently generated using combinatorial libraries based on robust protein scaffolds. αRep is such a family of artificial proteins, based on an α-solenoid protein repeat scaffold. The low aggregation propensity of the specific "binders" generated from this library opens new protein engineering opportunities such as the creation of biosensors within multidomain constructions. Here, we have explored the properties of two new types of artificial bidomain proteins based on αRep structures. Their structural and functional properties are characterized in detail using biophysical methods. The results clearly show that both bidomain proteins adopt a closed bivalve shell-like conformation, in the ligand free form. However, the

SUBMITTER: Leger C 

PROVIDER: S-EPMC6362204 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature