2qtu
From Proteopedia
Estrogen receptor beta ligand-binding domain complexed to a benzopyran ligand
Overview
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.
About this Structure
2QTU is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Benzopyrans as selective estrogen receptor beta agonists (SERBAs). Part 5: Combined A- and C-ring structure-activity relationship studies., Richardson TI, Dodge JA, Wang Y, Durbin JD, Krishnan V, Norman BH, Bioorg Med Chem Lett. 2007 Oct 15;17(20):5563-6. Epub 2007 Aug 11. PMID:17804226 Page seeded by OCA on Sun May 4 15:40:15 2008
Categories: Homo sapiens | Single protein | Dodge, J A. | Durbin, J D. | Krishnan, V. | Norman, B H. | Richardson, T I. | Wang, Y. | Alternative splicing | Dna-binding | Ligand-binding domain | Lipid-binding | Metal-binding | Nuclear receptor | Nucleus | Phosphorylation | Steroid-binding | Transcription | Transcription regulation | Transcription regulator | Zinc | Zinc-finger
