1X76: Crystal Structure Of Estrogen Receptor Beta Complexed With Way-697

Citation:
Abstract
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.
PDB ID: 1X76Download
MMDB ID: 31949
PDB Deposition Date: 2004/8/13
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 2.2  Å
Source Organism:
synthetic construct
Similar Structures:
Biological Unit for 1X76: tetrameric; determined by author and by software (PISA)
Molecular Components in 1X76
Label Count Molecule
Proteins (4 molecules)
2
Estrogen Receptor Beta(Gene symbol: ESR2)
Molecule annotation
2
Steroid Receptor Coactivator-1
Molecule annotation
Chemicals (2 molecules)
1
2
* Click molecule labels to explore molecular sequence information.

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