ArticleJournal of molecular modeling2017
Molecular dynamics simulations of asymmetric heterodimers of HER1/HER2 complexes.
Article in Journal of molecular modeling, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed, 1 citations in OpenAlex.
- Development andACS omega · 2026Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
The family of human epidermal growth factor receptors (HER) is involved in tumor cell growth. Homodimerization and heterodimerization of the HER family are important for activation of these receptors. The structures of homodimer conformation are well characterized, while the structures of heterodimer conformations, especially between HER1 and HER2, are not completely understood. In this study, two models of possible asymmetric HER1/HER2 kinase domains were built. Molecular dynamics simulations and molecular mechanics-Poisson-Boltzmann surface area (MM-PBSA) methods were applied to examine the possibility of these two-heterodimer interactions. From our results, it could be concluded that the HER2 kinase domain prefers to serve as the receiver rather than the activator. Key binding residues of this dimer complex at N lobe of HER2 is ALA683 and at C lobe of HER1 are GLU914, GLU917, and ASP930. This study will be useful in allowing us to predict and be able to control activity of this enzyme in disease in the future. Graphical abstract A model of the asymmetric dimer of HER1-HER2 heterodimer with key intereaction residues in (a) HER1A and (b) HER2R by molecular dynamic simulation.
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