Figure 2 | Scientific Reports

Figure 2

From: A novel function for globulin in sequestering plant hormone: Crystal structure of Wrightia tinctoria 11S globulin in complex with auxin

Figure 2

Protein-protein interaction involved in the formation of WTG hexamer. (A) The surface view of WTG trimer (yellow) showing the hydrophobic residues (red) involved in interaction with residues of another trimer. (B) The residue pairs of chain A and D involved in hydrogen bond formation. The N-terminal of chain A is stacked over C-terminal of chain D during hexamer formation. (C) The key residues involved in salt bridge formation between the trimers. Residues from chain A (orange sticks) and residues from chain D (green sticks). The interactions are shown via yellow dashed lines. (D) Residues His110, His128 and His152 present on the surface become more positively charged at acidic pH and result in dissociation of IE face. All residues have been shown in ball and stick representation.

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