Conformational selection in G-proteins: lessons from Ras and Rho.
Biophys J
; 99(11): L87-9, 2010 Dec 01.
Article
em En
| MEDLINE
| ID: mdl-21112273
ABSTRACT
The induced fit model has traditionally been invoked to describe the activating conformational change of the monomeric G-proteins, such as Ras and Rho. With this scheme, the presence or absence of the γ-phosphate of GTP leads to an instantaneous switch in conformation. Here we describe atomistic molecular simulations that demonstrate that both Ras and Rho superfamily members harbor an intrinsic susceptibility to sample multiple conformational states in the absence of nucleotide ligand. By comparing the distribution of conformers in the presence and absence of nucleotide, we show that conformational selection is the dominant mechanism by which Ras and Rho undergo nucleotide-dependent conformational changes. Furthermore, the pattern of correlated motions revealed by these simulations predicts a preserved allosteric coupling of the nucleotide-binding site with the membrane interacting C-terminus in both Rho and Ras.
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1
Base de dados:
MEDLINE
Assunto principal:
Proteínas ras
/
Proteínas rho de Ligação ao GTP
Tipo de estudo:
Prognostic_studies
Idioma:
En
Ano de publicação:
2010
Tipo de documento:
Article