Based on the folding conservation across the nuclear receptor superfamily and the sequence homology with RAR-gamma, we report the construction of a three dimensional model of the ligand binding domain of FXR. The model is exploited for the elucidation of the binding mode of 6alpha-ethyl-chenodeoxycholic acid. The results of the docking experiments give quite clear indications that the bile acid derivative would bind the receptor in a mode significantly different than that observed for agonists of other nuclear receptor superfamily.

Binding Mode of 6ECDCA, a Potent Bile Acid Agonist of the Farnesoid X Receptor (FXR)

COSTANTINO, Gabriele;MACCHIARULO, Antonio;CAMAIONI, Emidio;PELLICCIARI, Roberto
2003-01-01

Abstract

Based on the folding conservation across the nuclear receptor superfamily and the sequence homology with RAR-gamma, we report the construction of a three dimensional model of the ligand binding domain of FXR. The model is exploited for the elucidation of the binding mode of 6alpha-ethyl-chenodeoxycholic acid. The results of the docking experiments give quite clear indications that the bile acid derivative would bind the receptor in a mode significantly different than that observed for agonists of other nuclear receptor superfamily.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11391/149759
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