Molecular Modeling of Nearly Full-Length ErbB2 Receptor

作者: Péter Bagossi , Gábor Horváth , György Vereb , János Szöllösi , József Tözsér

DOI: 10.1529/BIOPHYSJ.104.046003

关键词:

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

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