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. 2019 Jun 20;116(28):13873–13878. doi: 10.1073/pnas.1905177116

Fig. 1.

Fig. 1.

Exosite II-targeting tick-derived thrombin inhibitors. (A) Cartoon representation of the complex between thrombin (gray) and madanin-1 (yellow) (Protein Data Bank entry 5L6N; ref. 14). The side chains of residues from the exosite I (orange), exosite II (blue), and the catalytic triad (red) of thrombin and of the sulfotyrosine-containing motif of madanin-1 (yellow) are represented as sticks. (B) Multiple amino acid sequence alignment of tick salivary proteins. The amino acid sequence of the sulfotyrosine-containing natural anticoagulant madanin-1 (14) (Mad1 – Q86FP9) from Haemaphysalis longicornis is aligned with those of madanin-like 1 (MadL1 – Q4R1A5) and madanin-like 2 (MadL2 – Q4R1A2) from the same organism; hyalomin 1 (Hya1 – E2J6S1), hyalomin 2 (Hya2 – E2J6T8), and hyalomin 3 (Hya3 – E2J6R9) from H. marginatum rufipes (22); and And82 and And310 [reported by Francischetti et al. (23)] from D. andersoni. The acidic sulfation motif is highlighted in yellow, with potential sulfation sites shown in inverted type on a red background. Other strictly conserved residues are shown in inverted type on a magenta background and moderately conserved residues on an orange background. Proposed ligation junctions are shown in inverted type on a black background.