1a52
From Proteopedia
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[[Image:1a52.gif|left|200px]] | [[Image:1a52.gif|left|200px]] | ||
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'''ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN COMPLEXED TO ESTRADIOL''' | '''ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN COMPLEXED TO ESTRADIOL''' | ||
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[[Category: Tanenbaum, D M.]] | [[Category: Tanenbaum, D M.]] | ||
[[Category: Wang, Y.]] | [[Category: Wang, Y.]] | ||
| - | [[Category: | + | [[Category: Estrogen]] |
| - | [[Category: | + | [[Category: Ligand]] |
| - | [[Category: | + | [[Category: Receptor]] |
| - | [[Category: | + | [[Category: Transcription regulation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:49:25 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 06:49, 2 May 2008
ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN COMPLEXED TO ESTRADIOL
Contents |
Overview
The 2.8-A crystal structure of the complex formed by estradiol and the human estrogen receptor-alpha ligand binding domain (hERalphaLBD) is described and compared with the recently reported structure of the progesterone complex of the human progesterone receptor ligand binding domain, as well as with similar structures of steroid/nuclear receptor LBDs solved elsewhere. The hormone-bound hERalphaLBD forms a distinctly different and probably more physiologically important dimer interface than its progesterone counterpart. A comparison of the specificity determinants of hormone binding reveals a common structural theme of mutually supported van der Waals and hydrogen-bonded interactions involving highly conserved residues. The previously suggested mechanism by which the estrogen receptor distinguishes estradiol's unique 3-hydroxy group from the 3-keto function of most other steroids is now described in atomic detail. Mapping of mutagenesis results points to a coactivator-binding surface that includes the region around the "signature sequence" as well as helix 12, where the ligand-dependent conformation of the activation function 2 core is similar in all previously solved steroid/nuclear receptor LBDs. A peculiar crystal packing event displaces helix 12 in the hERalphaLBD reported here, suggesting a higher degree of dynamic variability than expected for this critical substructure.
Disease
Known disease associated with this structure: Breast cancer OMIM:[133430], Estrogen resistance OMIM:[133430], Atherosclerosis, susceptibility to OMIM:[133430], HDL response to hormone replacement, augmented OMIM:[133430], Migraine, susceptibility to OMIM:[133430], Myocardial infarction, susceptibility to OMIM:[133430]
About this Structure
1A52 is a Single protein structure of sequence from Homo sapiens. The following page contains interesting information on the relation of 1A52 with [Estrogen Receptor]. Full crystallographic information is available from OCA.
Reference
Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains., Tanenbaum DM, Wang Y, Williams SP, Sigler PB, Proc Natl Acad Sci U S A. 1998 May 26;95(11):5998-6003. PMID:9600906 Page seeded by OCA on Fri May 2 09:49:25 2008
