1u9e

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spinqualitylabelsall models 1u9e, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF ESTROGEN RECEPTOR BETA COMPLEXED WITH WAY-397

Overview

We present the structure-based optimization of a series of estrogen, receptor-beta (ERbeta) selective ligands. X-ray cocrystal structures of, these ligands complexed to both ERalpha and ERbeta are described. We also, discuss how molecular modeling was used to take advantage of subtle, differences between the two binding cavities in order to optimize, selectivity for ERbeta over ERalpha. Quantum chemical calculations are, utilized to gain insight into the mechanism of selectivity enhancement., Despite only two relatively conservative residue substitutions in the, ligand binding pocket, the most selective compounds have greater than, 100-fold selectivity for ERbeta relative to ERalpha when measured using a, competitive radioligand binding assay.

About this Structure

1U9E is a Single protein structure of sequence from Homo sapiens with 397 as ligand. Full crystallographic information is available from OCA.

Reference

Structure-based design of estrogen receptor-beta selective ligands., Manas ES, Unwalla RJ, Xu ZB, Malamas MS, Miller CP, Harris HA, Hsiao C, Akopian T, Hum WT, Malakian K, Wolfrom S, Bapat A, Bhat RA, Stahl ML, Somers WS, Alvarez JC, J Am Chem Soc. 2004 Nov 24;126(46):15106-19. PMID:15548008

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