Fig. 3: Crystal structure of STL1267 bound to the ligand binding domain of REV-ERBα. | Nature Communications

Fig. 3: Crystal structure of STL1267 bound to the ligand binding domain of REV-ERBα.

From: Structural basis of synthetic agonist activation of the nuclear receptor REV-ERB

Fig. 3

a Crystal structure of STL1267 bound to the ligand binding domain of REV-ERBα with NCoR ID1. REV-ERBα is illustrated in green ribbons and NCoR ID1 in purple ribbons. The ligand is shown as ball and stick representation. Common structural components (α helices) within the nuclear receptor LBD are designated. b Close-up view of STL1267 binding within the ligand binding pocket of REV-ERBα. The ligand is illustrated as purple stick representation and the protein amino side chains are demonstrated by green stick representation. Hydrophobic amino acids stabilize STL1267 in the ligand binding pocket of REV-ERBα. c 2D diagram illustrating STL1267 interactions with amino acid residues within the ligand binding pocket of REV-ERBα. The label A corresponds to the REV-ERB protein residues while label B corresponds to the NCOR residues. (d) 2fo − fc electron density map around ST1267 contoured at 2σ.

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