Affinity of estrogens for human progesterone receptor A and B monomers and risk of breast cancer: a comparative molecular modeling study
Author(s) -
Tarique N. Hasan,
Masoodi,
Grace,
Shafi,
Ali A. Alshatwi
Publication year - 2011
Publication title -
advances and applications in bioinformatics and chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.223
H-Index - 15
ISSN - 1178-6949
DOI - 10.2147/aabc.s17371
Subject(s) - breast cancer , progesterone receptor , human breast , cancer , receptor , monomer , chemistry , estrogen receptor , endocrinology , medicine , organic chemistry , polymer
The human progesterone receptor (hPR) belongs to the steroid receptor family. It may be found as monomers (A and B) and or as a dimer (AB). hPR is regarded as the prognostic biomarker for breast cancer. In a cellular dimer system, AB is the dominant species in most cases. However, when a cell coexpresses all three isoforms of hPR, the complexity of the action of this receptor increases. For example, hPR A suppresses the activity of hPR B, and the ratio of hPR A to hPR B may determine the physiology of a breast tumor. Also, persistent exposure of hPRs to nonendogenous ligands is a common risk factor for breast cancer. Hence we aimed to study progesterone and some nonendogenous ligand interactions with hPRs and their molecular docking.
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