2QTU

Estrogen receptor beta ligand-binding domain complexed to a benzopyran ligand

2QTU の概要

• エントリーDOI: 10.2210/pdb2qtu/pdb
• 関連するPDBエントリー: 2I0G 2JJ3 2Z4B
• 分子名称: Estrogen receptor beta, (3aS,4R,9bR)-2,2-difluoro-4-(4-hydroxyphenyl)-6-(methoxymethyl)-1,2,3,3a,4,9b-hexahydrocyclopenta[c]chromen-8-ol (3 entities in total)
• 機能のキーワード: nuclear receptor, ligand-binding domain, alternative splicing, dna-binding, lipid-binding, metal-binding, nucleus, phosphorylation, steroid-binding, transcription, transcription regulation, zinc, zinc-finger, transcription regulator
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: Q92731
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59182.03

構造登録者

Richardson, T.I.,Dodge, J.A.,Wang, Y.,Durbin, J.D.,Krishnan, V.,Norman, B.H. (登録日: 2007-08-02, 公開日: 2007-10-30, 最終更新日: 2024-02-21)

主引用文献

Richardson, T.I.,Dodge, J.A.,Wang, Y.,Durbin, J.D.,Krishnan, V.,Norman, B.H.
Benzopyrans as selective estrogen receptor beta agonists (SERBAs). Part 5: Combined A- and C-ring structure-activity relationship studies.
Bioorg.Med.Chem.Lett., 17:5563-5566, 2007

PubMed Abstract: Benzopyrans are selective estrogen receptor (ER) beta agonists (SERBAs), which bind the ER subtypes alpha and beta in opposite orientations. Here we describe the synthesis of a late stage intermediate that allowed us to combine A-ring and C-ring modifications and carry out simultaneous SAR studies at both positions. Modification of both positions proved additive, maintaining affinity and improving ERbeta selectivity up to 83-fold. An X-ray cocrystal structure confirms the previously observed binding mode in ERbeta.

PubMed: 17804226
DOI: 10.1016/j.bmcl.2007.08.009

実験手法

X-RAY DIFFRACTION (2.53 Å)