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Molecular Modeling of Nearly Full-Length ErbB2 Receptor

Péter Bagossi ^*, Gábor Horváth , György Vereb , János Szöllösi   and József Tözsér ^*

Departments of ^* Biochemistry and Molecular Biology, Biophysics and Cell Biology, and Cell Biophysical Research Group of Hungarian Academy of Sciences, Research Center for Molecular Medicine, Medical and Health Science Center, University of Debrecen, Hungary

Correspondence: Address reprint requests to Péter Bagossi, the Department of Biochemistry and Molecular Biology, Research Center for Molecular Medicine, Medical and Health Science Center, University of Debrecen, H-4012 Debrecen, POB 6, Hungary. Tel.: 36-52-416-432; Fax: 36-52-314-989; E-mail: peter{at}indi.biochem.dote.hu.

Members of the epidermal growth factor receptor family play important roles in various cellular processes, both in physiological and in pathological conditions. Dimerization and autophosphorylation of these receptor tyrosine kinases are key events of signal transduction. Details of the molecular events of the signaling are not entirely known. To facilitate the understanding of receptor structure and function at the molecular level, a molecular model was built for the nearly full-length ErbB2 dimer. Modeling was based on the x-ray or nuclear-magnetic resonance structures of extracellular, transmembrane, and intracellular domains. The extracellular domain was positioned above the cell membrane based on the distance determined from experimentally measured fluorescence resonance energy transfer. Favorable dimerization interactions are predicted for the extracellular, transmembrane, and protein kinase domains in the model of a nearly full-length dimer of ErbB2, which may act in a coordinated fashion in ErbB2 homodimerization, and also in heterodimers of ErbB2 with other members of the ErbB family.