2qe4
Estrogen receptor alpha ligand-binding domain in complex with a benzopyran agonistEstrogen receptor alpha ligand-binding domain in complex with a benzopyran agonist
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBenzopyrans 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. 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 Sep 15;17(18):5082-5. Epub 2007 Jul 13. PMID:17662603[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Homo sapiens
- Dinn, S R.
- Dodge, J A.
- Durbin, J D.
- Durst, G L.
- Krishnan, V.
- Liu, S Q.
- Norman, B H.
- Pfeifer, L A.
- Reilly, J E.
- Richardson, T I.
- Ryter, K T.
- Wang, Y.
- Dna-binding
- Ligand-binding domain
- Lipid-binding
- Metal-binding
- Nuclear protein
- Nuclear receptor
- Phosphorylation
- Steroid-binding
- Transcription
- Transcription regulation
- Zinc-finger