Methods to Determine Interaction Interfaces Between ß-Arrestins and Their Protein Partners.
Methods Mol Biol
; 1957: 177-194, 2019.
Article
en En
| MEDLINE
| ID: mdl-30919355
ABSTRACT
ß-arrestins are so-called hub proteins they make complexes with many different partners, assembling functional complexes, and thereby fulfilling their biological function. The importance of this process in G protein-coupled receptor (GPCR) signalling has been fully demonstrated for many different receptors. For direct interactions, determining the interface regions, on ß-arrestins and on the partners, is crucial for understanding the function of the complex. Indeed, this brings information on which proteins can interact simultaneously with ß-arrestins, or, on the contrary, which partners are exclusive. We present here a method in two steps:
protein-protein docking allows finding a limited number of peptides predicted to be involved in the interaction, and then experimental approaches that might be used for validating the prediction.Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Beta-Arrestinas
/
Biología Molecular
Tipo de estudio:
Prognostic_studies
Límite:
Humans
Idioma:
En
Revista:
Methods Mol Biol
Asunto de la revista:
BIOLOGIA MOLECULAR
Año:
2019
Tipo del documento:
Article
País de afiliación:
Francia