Skip to main content
. 2004 Jul 25;9(15):659–669. doi: 10.1016/S1359-6446(04)03196-4

Figure 4.

Figure 4

(a,b) Comparison of the two isotypes of the estrogen receptor. In the homology model, ERα (blue) and ERβ (green) ligand-binding pockets are shown in complex with the natural ligand of the ER, 17β-estradiol. The binding of 8β-VE2, a highly potent and selective ERβ agonist, modeled into the ERβ ligand-binding niche is depicted to the right. Reproduced, with permission, from Ref. [31]. (c,d) A model of the antiprogestin RU 486 (Mifepristone) bound to hPR. A single amino acid mutation renders this compound inactive at the cPR and hamster PR. Steric clashes between RU 486 and cPR are shown on the right side. Abbreviations: ER, estrogen receptor; hER, human estrogen receptor; cPR, chicken progesterone receptor; hPR, human progesterone receptor; PR, progesterone receptor; RBA, relative binding affinity; 8β-VE2, 8β-vinylestra-1,3,5(10)-triene-3,17β-diol.