Design of stimulus-responsive two-state hinge proteins.
Science
; 381(6659): 754-760, 2023 08 18.
Article
em En
| MEDLINE
| ID: mdl-37590357
ABSTRACT
In nature, proteins that switch between two conformations in response to environmental stimuli structurally transduce biochemical information in a manner analogous to how transistors control information flow in computing devices. Designing proteins with two distinct but fully structured conformations is a challenge for protein design as it requires sculpting an energy landscape with two distinct minima. Here we describe the design of "hinge" proteins that populate one designed state in the absence of ligand and a second designed state in the presence of ligand. X-ray crystallography, electron microscopy, double electron-electron resonance spectroscopy, and binding measurements demonstrate that despite the significant structural differences the two states are designed with atomic level accuracy and that the conformational and binding equilibria are closely coupled.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Engenharia de Proteínas
Idioma:
En
Ano de publicação:
2023
Tipo de documento:
Article