2p15: Difference between revisions

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{{STRUCTURE_2p15|  PDB=2p15  |  SCENE=  }}  
{{STRUCTURE_2p15|  PDB=2p15  |  SCENE=  }}  


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




==Overview==
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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.
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{{ABSTRACT_PUBMED_17468738}}


==About this Structure==
==About this Structure==
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[[Category: Ligand binding domain]]
[[Category: Ligand binding domain]]
[[Category: Nulear receptor]]
[[Category: Nulear receptor]]
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