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. 2017 Aug 9;15(9):1818–1828. doi: 10.1111/jth.13773

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© 2017 The Authors. Journal of Thrombosis and Haemostasis published by Wiley Periodicals, Inc. on behalf of International Society on Thrombosis and Haemostasis.

This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

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Charge surface representations of the activated factor XII (FXIIa)–corn trypsin inhibitor (CTI) interaction (blue = positive, red = negative). (A) The FXIIa model is shown with the key surface pockets labeled. (B) Docked complex of FXIIa (shown as a cartoon in gray) and CTI shown as a transparent charged surface illustrating the basic region interacting with the negatively charged S1 (D189) and H1 (D60) residues shown as sticks. (C) FXIIa protease as viewed in (A) but with CTI residues 20–44 shown as a cartoon in cyan, with key residues labeled as sticks in cyan.