Fig. 3.

Recognition mechanism of AtLURE1.2 by AtPRK6^LRR. a A close-up view of binding of the C-terminal side from AtPRK6^LRR to a positively charged surface of AtLURE1.2. AtLURE1.2 is shown in transparent electrostatic surface. Some of the critical amino acids from AtPRK6^LRR and AtLURE1.2 are shown in stick. Squares in three different colors indicate the interfaces between AtPRK6^LRR and AtLURE1.2. b The C-terminal side of AtPRK6^LRR binds to a hydrophobic cavity formed between the α-helix and the second β-sheet of AtLURE1.2. Red lines indicate hydrogen bonds. The red sphere represents water molecule. c Arg83 of AtLURE1.2 is at the center of the AtLURE1.2-AtPRK6^LRR interface and form extensive interactions with AtPRK6^LRR. d A network of polar interactions is formed between Asp234 of AtPRK6 and AtLURE1.2