2qe4
From Proteopedia
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Estrogen receptor alpha ligand-binding domain in complex with a benzopyran agonist
Contents |
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 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 Sep 15;17(18):5082-5. Epub 2007 Jul 13. PMID:17662603
Page seeded by OCA on Thu Feb 21 18:38:29 2008
Categories: Homo sapiens | Single protein | 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. | JJ3 | Alternative splicing | Dna-binding | Ligand-binding domain | Lipid-binding | Metal-binding | Nuclear protein | Nuclear receptor | Phosphorylation | Polymorphism | Steroid-binding | Transcription | Transcription regulation | Zinc | Zinc-finger
