taurochenodeoxycholic-acid and obeticholic-acid

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.

Topics: Amino Acid Sequence; Bile Acids and Salts; Binding Sites; Chenodeoxycholic Acid; DNA-Binding Proteins; Humans; Models, Molecular; Molecular Sequence Data; Protein Binding; Receptors, Cytoplasmic and Nuclear; Receptors, Retinoic Acid; Sequence Alignment; Sequence Homology, Amino Acid; Transcription Factors