Structural similarities between HvPYR/PYL5, HvPYR/PYL1, and HvPYR/PYL2 and two members of the Arabidopsis RCAR/PYR/PYL family. Three-dimensional models have been generated using I-TASSER and further processed with PyMOL software. A, Amino acid sequence alignment. Identical residues are indicated by asterisks, and predicted α-helical and β-sheet structures are highlighted in red and blue, respectively. Remaining residues are coils. B, C, and D, Predicted three-dimensional models (best score) of HvPYR/PYL5 (B), HvPYR/PYL1 (C), and HvPYR/PYL2 (D). At left, N and C termini are indicated, and gate and latch regions are shown in white. The middle shows an overlay with the top hit structural Arabidopsis analog (AtPYL2 for HvPYR/PYL5 and HvPYR/PYL1, AtPYR1 for HvPYR/PYL2) generated with PyMOL. Green indicates the HvPYR/PYL sequence, white indicates the Arabidopsis RCAR/PYR/PYL sequence, and orange- and magenta-labeled residues indicate different amino acids at that position. At right, predicted ligand binding sites within the gate and latch regions and amino acid residues and their position within the protein sequence are indicated.