Unique ligand binding patterns between estrogen receptor alpha and beta revealed by hydrogen-deuterium exchange.

ABSTRACT: Here we present the use of hydrogen-deuterium exchange (HDX) mass spectrometry in analyzing the estrogen receptor beta ligand binding domain (ERbeta LBD) in the absence and presence of a variety of chemical compounds with different binding modes and pharmacological properties. Previously, we reported the use of HDX as a method for predicting the tissue selectivity of ERalpha ligands. HDX profiles of ERalpha LBD in complex with ligand could differentiate compounds of the same chemotype. In contrast, similar analysis of ERbeta LBD showed correlation to the compound chemical structures but little correlation with compound tissue selectivity. The different HDX patterns observed for ERbeta LBD when compared to those for ERalpha LBD bound to the same chemical compounds serve as an indication tha

SUBMITTER: Dai SY 

PROVIDER: S-EPMC2782520 | biostudies-literature | 2009 Oct

REPOSITORIES: biostudies-literature