Spatial Structure of the Dimeric Transmembrane Domain of the Growth Factor Receptor ErbB2 Presumably Corresponding to the Receptor Active State
Eduard V. Bocharov(Institute of Bioorganic Chemistry), Константин С. Минеев(Institute of Bioorganic Chemistry), Pavel E. Volynsky(Institute of Bioorganic Chemistry), Yaroslav S. Ermolyuk(Institute of Bioorganic Chemistry), Elena N. Tkach(Institute of Bioorganic Chemistry), Alexander G. Sobol(Institute of Bioorganic Chemistry), Vladimir Chupin(Institute of Bioorganic Chemistry), М. П. Кирпичников(Institute of Bioorganic Chemistry), Roman G. Efremov(Institute of Bioorganic Chemistry), Alexander S. Arseniev(Institute of Bioorganic Chemistry)
Cited by 206Open Access
Abstract
Proper lateral dimerization of the transmembrane domains of receptor tyrosine kinases is required for biochemical signal transduction across the plasma membrane. The spatial structure of the dimeric transmembrane domain of the growth factor receptor ErbB2 embedded into lipid bicelles was obtained by solution NMR, followed by molecular dynamics relaxation in an explicit lipid bilayer. ErbB2 transmembrane segments associate in a right-handed alpha-helical bundle through the N-terminal tandem GG4-like motif Thr652-X3-Ser656-X3-Gly660, providing an explanation for the pathogenic power of some oncogenic mutations.
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