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PMID: 15596490 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Molecular modeling of nearly full-length ErbB2 receptor.

Biophysical journal ·Vol. 88 ·No. 2 ·2005-02-00 ·Pages 1354-63

Bagossi P, Horváth G, Vereb G, Szöllösi J, Tözsér J

Abstract

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.

MeSH Terms
Cell Line, Tumor Computer Simulation Dimerization Fluorescence Resonance Energy Transfer/methods Humans Lipid Bilayers/chemistry Models, Chemical Models, Molecular Neoplasms/chemistry,ultrastructure Protein Conformation Protein Structure, Tertiary Receptor, ErbB-2/analysis,chemistry,ultrastructure Structure-Activity Relationship
Chemicals
Lipid Bilayers Receptor, ErbB-2
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Bagossi Péter
Department of Biochemistry, Research Center for Molecular Medicine, Medical and Health Science Center, University of Debrecen, Hungary. peter@indi.biochem.dote.hu
Horváth Gábor
Vereb György
Szöllösi János
Tözsér József
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Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
DOI
10.1529/biophysj.104.046003
Email
peter@indi.biochem.dote.hu
Published
2005-02-00
Epub
2004-00-13
Pages
1354-63
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1305137
Subset
IM
External Links
PubMed source DOI: 10.1529/biophysj.104.046003 PMC Full Text View journal details
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