ETUDE DU DOMAINE TRANSMEMBRANAIRE DE RECEPTEUR TYROSINE KINASE DANS UN ENVIRONNEMENT MEMBRANAIRE. ASPECTS STRUCTURAUX ET MECANISTIQUES EXPLORES PAR DYNAMIQUE MOLECULAIRE

Abstract : Ligand-induced dimerization is necessary for tyrosine kinase receptor activation. The unique transmembrane domain of these proteins plays a crucial role in these mechanisms. The rodent Neu receptor and its human homologous ErbB2 are involved in several cancers induced by the Val to Glu substitution in the transmembrane domain or by overexpression. The structureof the transmembrane domain in the receptor dimer is a key determinant for dimerization and activation processes. Molecular dynamics simulations performed in hydrated DMPC and POPC membranes show that the transmembrane helices of the wild and the oncogenic Neu receptor form a left-handed structure with a symmetrical helix-helix interface. In the oncogenic form of Neu, the polar Glu residue is embedded into the membrane and stabilizes helix-helix interactions by forming strong inter helical hydrogen bonds.
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https://tel.archives-ouvertes.fr/tel-00009393
Contributor : Patricia Leloup <>
Submitted on : Thursday, August 4, 2005 - 12:14:22 PM
Last modification on : Wednesday, June 27, 2018 - 8:24:02 AM
Long-term archiving on : Monday, September 20, 2010 - 12:51:14 PM

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  • HAL Id : tel-00009393, version 2

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Pierre Aller. ETUDE DU DOMAINE TRANSMEMBRANAIRE DE RECEPTEUR TYROSINE KINASE DANS UN ENVIRONNEMENT MEMBRANAIRE. ASPECTS STRUCTURAUX ET MECANISTIQUES EXPLORES PAR DYNAMIQUE MOLECULAIRE. domain_other. Université d'Orléans, 2004. Français. ⟨tel-00009393v2⟩

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