Partenaires

CNRS


Rechercher


Accueil > Publications > Recherche par années > Années 2000 > 2001

Sajot, N ; Genest, M

Dimer interface of transmembrane domains for neu/erbB-2 receptor dimerization and transforming activation : a model revealed by molecular dynamics simulations

Journal of Biomolecular Structure & Dynamics, 19 (1) 15-31

par Administrateur - publié le , mis à jour le

Abstract :

The specific point mutation Val —> Glu664 within the transmembrane domain of the neu/erbB-2 receptor is associated with increased receptor dimerization and increased receptor tyrosine kinase activity resulting in malignant transformation of cells. It is well established that Glu and residues in proximity are necessary for receptor dimerization but many studies suggest that other intramembrane constraints, not yet elucidated, are determinant for transformation. In this work. we investigated dimer models both to understand the structural role of the Glu mutation in the transmembrane domain association and to determine helix-helix contacts required for oncogenic transformation.