2p15

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[[Image:2p15.gif|left|200px]]<br /><applet load="2p15" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2p15.gif|left|200px]]
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caption="2p15, resolution 1.940&Aring;" />
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'''Crystal structure of the ER alpha ligand binding domain with the agonist ortho-trifluoromethylphenylvinyl estradiol'''<br />
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{{Structure
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|PDB= 2p15 |SIZE=350|CAPTION= <scene name='initialview01'>2p15</scene>, resolution 1.940&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=EZT:(17BETA)-17-{(E)-2-[2-(TRIFLUOROMETHYL)PHENYL]VINYL}ESTRA-1(10),2,4-TRIENE-3,17-DIOL'>EZT</scene>
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|ACTIVITY=
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|GENE= ESR1, ESR, NR3A1 ([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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'''Crystal structure of the ER alpha ligand binding domain with the agonist ortho-trifluoromethylphenylvinyl estradiol'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2P15 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=EZT:'>EZT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P15 OCA].
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2P15 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P15 OCA].
==Reference==
==Reference==
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Structural plasticity in the oestrogen receptor ligand-binding domain., Nettles KW, Bruning JB, Gil G, O'Neill EE, Nowak J, Guo Y, Kim Y, DeSombre ER, Dilis R, Hanson RN, Joachimiak A, Greene GL, EMBO Rep. 2007 Jun;8(6):563-8. Epub 2007 Apr 27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17468738 17468738]
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Structural plasticity in the oestrogen receptor ligand-binding domain., Nettles KW, Bruning JB, Gil G, O'Neill EE, Nowak J, Guo Y, Kim Y, DeSombre ER, Dilis R, Hanson RN, Joachimiak A, Greene GL, EMBO Rep. 2007 Jun;8(6):563-8. Epub 2007 Apr 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17468738 17468738]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: nulear receptor]]
[[Category: nulear receptor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:24:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:07:11 2008''

Revision as of 16:07, 20 March 2008


PDB ID 2p15

Drag the structure with the mouse to rotate
, resolution 1.940Å
Ligands:
Gene: ESR1, ESR, NR3A1 (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the ER alpha ligand binding domain with the agonist ortho-trifluoromethylphenylvinyl estradiol


Contents

Overview

The steroid hormone receptors are characterized by binding to relatively rigid, inflexible endogenous steroid ligands. Other members of the nuclear receptor superfamily bind to conformationally flexible lipids and show a corresponding degree of elasticity in the ligand-binding pocket. Here, we report the X-ray crystal structure of the oestrogen receptor alpha (ERalpha) bound to an oestradiol derivative with a prosthetic group, ortho- trifluoromethlyphenylvinyl, which binds in a novel extended pocket in the ligand-binding domain. Unlike ER antagonists with bulky side groups, this derivative is enclosed in the ligand-binding pocket, and acts as a potent agonist. This work shows that steroid hormone receptors can interact with a wider array of pharmacophores than previously thought through structural plasticity in the ligand-binding pocket.

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

2P15 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural plasticity in the oestrogen receptor ligand-binding domain., Nettles KW, Bruning JB, Gil G, O'Neill EE, Nowak J, Guo Y, Kim Y, DeSombre ER, Dilis R, Hanson RN, Joachimiak A, Greene GL, EMBO Rep. 2007 Jun;8(6):563-8. Epub 2007 Apr 27. PMID:17468738

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