Fig. 2: Overall structure of hTAAB Fab in complex with Tie2 Fn2–3.

a Overall structure of the 2:2 hTie2 Fn2–3/chimeric hTAAB Fab complex. The 2-fold axis of the dimeric complex is indicated as a black ellipse. The heavy and light chains of chimeric hTAAB Fab are colored in dark and light orange, respectively. The hTie2 Fn2–3 dimer is colored in teal and cyan. b Sequence comparison of human and mouse Tie2 Fn2–3 domains. The dots in the mouse Tie2 sequence indicate residues that are identical to human Tie2. c The surface representations are open-book views showing the interacting interfaces of Tie2 Fn2–3 (top) and chimeric hTAAB Fab (bottom). The color scheme of hTie2 Fn2–3 and chimeric hTAAB Fab is identical to that in (a), but inverted for their respective binding surface. Six CDR loops of chimeric hTAAB Fab are indicated with different color lines (bottom). d Sequence comparison of the variable region of hTAAB heavy (top) and light (bottom) chains with closest human and mouse variable region germline genes. The dots in mouse and human germline sequences indicate the residues that are identical to hTAAB. b–d hTie2 residues that interact with the heavy and light chain of chimeric hTAAB Fab are colored dark and light orange, respectively, and V730, which interacts with both heavy and light chains, is highlighted in red (b, c, top). The chimeric hTAAB Fab residues that interact with hTie2 Fn3 are colored cyan (c, bottom, and d).