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. 2014 May 28;16(3):R53. doi: 10.1186/bcr3664

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Copyright © 2014 Aguilar et al.; licensee BioMed Central Ltd.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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YC-1 binds to estrogen receptor α. (A) Chemical structures of WAY-169916, WAY6 and YC-1. (B) Predicted binding mode of YC-1 (purple) in the partially constrained conformation of estrogen receptor α (ERα) (chain A, Protein Data Bank code 3OS8 [Swiss-Prot:P03372]). The binding mode of WAY6 (white sticks) is shown as a reference. (C) The results of the ERα agonist fluoligand assay using YC-1 are shown, along with the concentration–inhibition curve with duplicates. *YC-1 was not completely soluble at concentrations >100 μM.