Dimérisation du domaine transmembranaire des récepteurs de la famille ErbB/HER. Etude par simulations de dynamique moléculaire.

Abstract : ErbBjHER proteins belong to receptor tyrosine kinase family and are involved in a complex interaction network at the cell surface which control cellular proliferation and differentiation. This family of four members (ErbBljEGFR, ErbB2, ErbB3, ErbB4) forms homodimers andj or heterodimers after ligand binding. The deregulation of ErbB interaction network is associated with a variety of human cancers.
The transmembrane domain plays an important role in receptor function and the role of the GxxxG-like motif in oligomerization processes is of great interest. Experimental studies show a correlation between the hierarchy of the interaction of the whole receptors and that of the transmembrane domains. .
Theoretical search model has been developed to define structural models of heterodimers. Interactions between the transmembrane domains have been quantified and the role of the dimerization motifs has been determined. Molecular dynamics simulations show a preference for left-handed interactions of the two helices and the small residues of the motifs are found at the helix-helix interface. OUf studies show that the transmembrane domains are involved in receptor specificity and selectivity in dimerization processes.
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Submitted on : Monday, October 13, 2008 - 4:17:02 PM
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  • HAL Id : tel-00329923, version 1

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Oumarou Samna Soumana. Dimérisation du domaine transmembranaire des récepteurs de la famille ErbB/HER. Etude par simulations de dynamique moléculaire.. domain_other. Université d'Orléans, 2007. Français. ⟨tel-00329923⟩

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