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Duan, Y., Wu, C., Chowdhury, S., Lee, M.C., Xiong, G., Zhang, W., Yang, R., Cieplak, P., Luo, R., Lee, T., Caldwell, J., Wang, J. and Kollman, P. (2003) A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations. Journal of Computational Chemistry, 24, 1999-2012. doi:10.1002/jcc.10349
has been cited by the following article:
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TITLE:
More Stable, More Estrogenic: The SERM-ERα LBD Complex
AUTHORS:
Li Gao, Yaoquan Tu, Leif A. Eriksson
KEYWORDS:
Breast Cancer; Tamoxifen Resistance; Molecular Dynamics Simulations;
Dihydrobenzoxathiin; SERM
JOURNAL NAME:
Journal of Biophysical Chemistry,
Vol.2 No.3,
August
9,
2011
ABSTRACT: Many synthetic selective estrogen receptor modulators (SERMs) have been cocrystallized with the human estrogen receptor α ligand binding domain (ERα LBD). Despite stabilizing the same canonical inactive conformation of the LBD, most SERMs display different ligand-dependent pharmacological profiles. We show here that increased partial agonism of SERMs is associated with increased conformational stability of the SERM-LBD complexes, by investigation of dihydrobenzoxathiin-based SERMs using molecular modelling techniques. Analyses of tamoxifen (TAM) and 4-hydroxytamoxifen (OHT) in complex with the LBD furthermore indicates that the conversion of TAM to OHT increases both the affinity to ERα and the partial agonism of the anti-cancer drug, which provides a plausible explanation of the counterintuitive results of TAM therapy.
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