Journal
MOLECULAR INFORMATICS
Volume 32, Issue 7, Pages 647-658Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/minf.201200136
Keywords
GPER; Homology modeling; Agonism; Antagonism
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Funding
- NIDA NIH HHS [R21 DA037096, R01 DA024022] Funding Source: Medline
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G protein-coupled estrogen receptor (GPER) has been shown to be important in several disease states such as estrogen sensitive cancers. While several selective ligands have been identified for the receptor, little is known about how they interact with GPER and how their structures influence their activity. Specifically, within one series of ligands, whose structure varied only at one position, the replacement of a hydrogen atom with an acetyl group changed a potent antagonist into a potent agonist. In this study, two GPER homology models were constructed based on the X-ray crystal structures of both the active and inactive (2)-adrenergic receptors ((2)AR) in an effort to characterize the differences of binding modes between agonists and antagonists to the receptor, and to understand their activity in relation to their structures. The knowledge attained in this study is expected to provide valuable information on GPER ligands structure activity relationship to benefit future rational design of potent agonists and antagonists of the receptor for potential therapeutic applications.
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