Fig. 3: Interactions of Tie2 Fn3 with hTAAB and homotypic Fn3 interactions. | Nature Communications

Fig. 3: Interactions of Tie2 Fn3 with hTAAB and homotypic Fn3 interactions.

From: Structural insights into the clustering and activation of Tie2 receptor mediated by Tie2 agonistic antibody

Fig. 3

a Close-up view of key molecular interactions (A, B and C regions). Residues involved in the hTie2 Fn3/chimeric hTAAB Fab interaction (red, green, and blue boxes) and hTie2 dimerization (black box) are displayed as sticks and labeled. Hydrogen bonds and electrostatic interactions are indicated by dashed lines. b Key amino acid residues of A, B, and C regions involved in hTAAB binding. Interaction residues of hTAAB are listed on the left, and the corresponding interaction residues of Tie2 are listed on the right. Interactions between residue partners are indicated in red (ionic interaction), black (hydrogen bond), and blue (hydrophobic interaction). c Electrostatic potential of the hTie2 Fn2–3/chimeric hTAAB Fab complex, calculated according to the Poisson–Boltzmann equation in PyMOL. The structures are shown as open-book views and surface representations, with color maps reflecting electrostatic properties (blue, positively charged; red, negatively charged). The interacting regions are highlighted by a yellow line. d Hydrophobic residues in hTie2 Fn2–3 and chimeric hTAAB Fab are presented on the surface, and the interaction interface is marked with a black line.

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