2qe4

From Proteopedia

proteopedia linkproteopedia link

spinqualitylabelsall models 2qe4, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Estrogen receptor alpha ligand-binding domain in complex with a benzopyran agonist

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

Benzopyrans are selective estrogen receptor (ER) beta agonists (SERBAs), which bind the ER receptor subtypes alpha and beta in opposite, orientations. We have used structure based drug design to show that this, unique phenomena can be exploited via substitution at the 8-position of, the benzopyran A-ring to disrupt binding to ERalpha, thus improving ERbeta, subtype selectivity. X-ray cocrystal structures with ERalpha and ERbeta, are supportive of this approach to improve selectivity in this structural, class.

Disease

Known diseases associated with this structure: Atherosclerosis, susceptibility to OMIM:[133430], Breast cancer OMIM:[133430], Estrogen resistance OMIM:[133430], HDL response to hormone replacement, augmented OMIM:[133430], Migraine, susceptibility to OMIM:[133430], Myocardial infarction, susceptibility to OMIM:[133430]

About this Structure

2QE4 is a Single protein structure of sequence from Homo sapiens with JJ3 as ligand. Full crystallographic information is available from OCA.

Reference

Benzopyrans as selective estrogen receptor beta agonists (SERBAs). Part 4: Functionalization of the benzopyran A-ring., Norman BH, Richardson TI, Dodge JA, Pfeifer LA, Durst GL, Wang Y, Durbin JD, Krishnan V, Dinn SR, Liu S, Reilly JE, Ryter KT, Bioorg Med Chem Lett. 2007 Jul 13;. PMID:17662603

Page seeded by OCA on Mon Nov 12 23:32:33 2007