Quaternary structure predictions and structural communication features of GPCR dimers.
Prog Mol Biol Transl Sci
; 117: 105-42, 2013.
Article
en En
| MEDLINE
| ID: mdl-23663967
In spite of the ever-increasing evidence that G protein-coupled receptors (GPCRs) form dimers/oligomers, the biological role(s) and structural architecture of homologous and heterologous receptor aggregation are, however, far from being clarified. This chapter reviews the insights gained so far, at multiscale levels of resolution, on GPCR dimerization/oligomerization from in vitro experiments, structure predictions, and structure determinations. Focus is put on the achievement by the FiPD-based approach, which proved effective in predicting the supramolecular organization of membrane proteins including GPCRs. The combination of FiPD-based quaternary structure predictions with molecular simulations and analyses can be a valuable tool to infer the effects of dimerization on the structural communication features of a receptor dimer/oligomer bound to functionally different ligands. Ultimately, the integration between atomistic and mesoscopic simulations is expected to be a promising tool to unveil functioning mechanisms that involve intricate protein networks.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Biología Computacional
/
Receptores Acoplados a Proteínas G
/
Multimerización de Proteína
Tipo de estudio:
Prognostic_studies
/
Risk_factors_studies
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Prog Mol Biol Transl Sci
Asunto de la revista:
BIOLOGIA MOLECULAR
Año:
2013
Tipo del documento:
Article
País de afiliación:
Italia
Pais de publicación:
Países Bajos