2p15: Difference between revisions
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New page: left|200px<br /> <applet load="2p15" size="450" color="white" frame="true" align="right" spinBox="true" caption="2p15, resolution 1.940Å" /> '''Crystal structure ... |
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[[Image:2p15.gif|left|200px]]<br /> | [[Image:2p15.gif|left|200px]]<br /><applet load="2p15" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="2p15" size=" | |||
caption="2p15, resolution 1.940Å" /> | caption="2p15, resolution 1.940Å" /> | ||
'''Crystal structure of the ER alpha ligand binding domain with the agonist ortho-trifluoromethylphenylvinyl estradiol'''<br /> | '''Crystal structure of the ER alpha ligand binding domain with the agonist ortho-trifluoromethylphenylvinyl estradiol'''<br /> | ||
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==Overview== | ==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. | 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. | ||
==About this Structure== | ==About this Structure== | ||
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 EZT as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 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]. | ||
==Reference== | ==Reference== | ||
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[[Category: nulear receptor]] | [[Category: nulear receptor]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:28:54 2008'' | ||
