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. 2011 Jul 20;286(36):31225–31231. doi: 10.1074/jbc.M111.252916

FIGURE 2.

FIGURE 2.

The cofactor binding site of the FTZ-F1 LBD. A, left, the ribbon representation shows intermolecular interactions between the FTZ-F1 LBD and FTZPEP. The ribbon depiction of FTZPEP (pink) in the co-activator binding site of the FTZ-F1 LBD (yellow) is presented. Middle, the hydrophobic interaction patch between the FTZ-F1 LBD and FTZPEP is represented. Leucine resides Leu-109, Leu-112, and Leu-113 of FTZPEP are involved in hydrophobic contacts with the hydrophobic cluster formed by helices H3, H4, and H12 of the FTZ-F1 LBD. Right, the surface representation shows intermolecular interactions between the FTZ-F1 LBD and FTZPEP. All residues involved in interactions between the FTZ-F1 LBD and FTZPEP are represented by surface charge distribution. B, comparison of cofactor binding sites in proteins from NR5A family. Common charge clamps of FTZ-F1, LRH-1, and SF-1 LBD are shown, respectively. Residues in NR LBDs and in the cofactors are displayed in black and red, respectively.