1qkt

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spinqualitylabelsall models 1qkt, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

MUTANT ESTROGEN NUCLEAR RECEPTOR LIGAND BINDING DOMAIN COMPLEXED WITH ESTRADIOL

Overview

The crystal structure of a triple cysteine to serine mutant ERalpha, ligand-binding domain (LBD), complexed with estradiol, shows that despite, the presence of a tightly bound agonist ligand, the protein exhibits an, antagonist-like conformation, similar to that observed in raloxifen and, 4-hydroxytamoxifen-bound structures. This mutated receptor binds estradiol, with wild type affinity and displays transcriptional activity upon, estradiol stimulation, but with limited potency (about 50%). This partial, activity is efficiently repressed in antagonist competition assays. The, comparison with available LBD structures reveals key features governing, the positioning of helix H12 and highlights the importance of cysteine, residues in promoting an active conformation. Furthermore the present, ... [(full description)]

About this Structure

1QKT is a [Single protein] structure of sequence from [Homo sapiens] with EST as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Crystal structure of a mutant hERalpha ligand-binding domain reveals key structural features for the mechanism of partial agonism., Gangloff M, Ruff M, Eiler S, Duclaud S, Wurtz JM, Moras D, J Biol Chem. 2001 May 4;276(18):15059-65. Epub 2001 Feb 6. PMID:11278577

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