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. 2021 Jun 24;41(8):2263–2276. doi: 10.1161/ATVBAHA.121.316038

Figure 4.

Figure 4.

Comparison of interdomain hydrogen bonds between surfaces of the A2 and the A1/A3 domains in human and Pseudonaja textilis FV (factor V). The structural conformation and interdomain hydrogen bonds between the surfaces of the A2 and A1 (B–C, H–I) or A2 and A3 (E–F and K–L) domains are shown at the start (t=0 ns; B, E, H, and K) and end (t=100 ns; C, F, I, L) of the hFVa (human factor Va; B-C, E-F) and ptFVa-h306 S-S (H-I, K-L) MD simulations. The A1, A2, and A3 domains are indicated in blue, pink, and green, respectively. Residues that engage in hydrogen bond formation and the APC cleavage sites (hFVa, Arg306, Arg506; ptFVa, Arg307, Lys507) are shown in stick configuration, with the latter highlighted in red. Hydrogen bonds are indicated by the yellow dashed lines. The A1 domain loop1 and A2 domain loop2 represent the identified unique loop conformations. A, D, G, and J, Interdomain hydrogen bonds between the A2 and A1 (A and G) or A2 and A3 (D and J) domains were quantified during a 100 ns MD simulation of hFVa (A and D) and ptFVa (Pseudonaja textilis venom-derived factor V)-h306 S-S (G and J).