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. 2013 Oct 25;13:27. doi: 10.1186/1472-6807-13-27

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Copyright © 2013 Chakraborty 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/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Structures of RES-ERα complexes obtained from MD simulation. (A) The structures of RES-ERαagonist (green) and RES-ERαantagonist (red) are overlapped. Using VMD, the ERα is shown in New Cartoon representation, and RES is shown in VDW mode. The side chains of some of the residues whose conformations are dramatically different between the complexes are shown: Helix12 and linker region of Helices 8 and 9. (B) &(C) Details of the hydrogen bonding contacts between DES and RES with ERα agonist conformation, respectively. RES is bound within the same ERα pocket that recognizes DES and 4OHT [30,32,33]. The hydrogen-bonding interactions with the different residues are shown.