1a52

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[[Image:1a52.gif|left|200px]]<br /><applet load="1a52" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1a52.gif|left|200px]]
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caption="1a52, resolution 2.8&Aring;" />
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'''ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN COMPLEXED TO ESTRADIOL'''<br />
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{{Structure
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|PDB= 1a52 |SIZE=350|CAPTION= <scene name='initialview01'>1a52</scene>, resolution 2.8&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=EST:ESTRADIOL'>EST</scene> and <scene name='pdbligand=AU:GOLD ION'>AU</scene>
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|ACTIVITY=
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|GENE= ESR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN COMPLEXED TO ESTRADIOL'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1A52 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=EST:'>EST</scene> and <scene name='pdbligand=AU:'>AU</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1A52 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb45_1.html Estrogen Receptor]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A52 OCA].
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1A52 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 1A52 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb45_1.html Estrogen Receptor]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A52 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9600906 9600906]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9600906 9600906]
[[Category: Estrogen Receptor]]
[[Category: Estrogen Receptor]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: transcription regulation]]
[[Category: transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:40:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:53:01 2008''

Revision as of 07:53, 20 March 2008

Image:1a52.gif


PDB ID 1a52

Drag the structure with the mouse to rotate
, resolution 2.8Å
Ligands: and
Gene: ESR (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



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 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

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

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