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. 2019 Jun 17;17(8):1229–1239. doi: 10.1111/jth.14487

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© 2019 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 http://creativecommons.org/licenses/by-nc-nd/4.0/ License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.

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The factor Va C1 and C2 domains facilitate interaction with the anionic lipid membrane surface. A zoomed‐in region of the human ternary model by Shim et al. is shown38; the insert outlines the specific region depicted. The hydrophobic protruding spikes of the C1 and C2 domains (shown in stick configuration) insert into the anionic lipid membrane layer. Additional interactions are provided by the groove between the C domains (residues spanning Lys1954‐Arg2027 and Lys2060‐Arg2187, specified at Tables S6 and S7). FVa amino acids implicated as contact residues are indicated in pink, FVa is indicated in teal. See Movie S7 for a 3D overview. Abbreviations: FVa, factor Va; FXa, factor Xa