Figure 4
(A) Sequence alignment of the C3C4 region comparing wild-type Inf4 and AaTI. The four different residues are underlined. The P14′ residue, Gly25, on Inf4 is colored red. (B) Ribbon and the corresponding surface diagram of the model complex structure between Inf4 (gray) and FXIIa (beige) showing the surface loops of FXIIa: 37-loop (green), 60-loop (purple), 99-loop (orange), 140-loop (cyan), 186-loop (yellow) and 220-loop (blue) as stated in Dementiev et al. (2018). The Gly25 (P14′) residue of Inf4 is shown in red color and the Tyr151 residue of FXIIa is shown as a cyan stick model. (C) A different view of the ribbon and corresponding surface diagram of the model of the Inf4-FXIIa complex. The color scheme is as described in (B). The diagrams are generated by the program UCSF Chimera.
Ribbon and surface diagrams of the Inf4-FXIIa complex model

(A) Sequence alignment of the C3C4 region comparing wild-type Inf4 and AaTI. The four different residues are underlined. The P14′ residue, Gly25, on Inf4 is colored red. (B) Ribbon and the corresponding surface diagram of the model complex structure between Inf4 (gray) and FXIIa (beige) showing the surface loops of FXIIa: 37-loop (green), 60-loop (purple), 99-loop (orange), 140-loop (cyan), 186-loop (yellow) and 220-loop (blue) as stated in Dementiev et al. (2018). The Gly25 (P14′) residue of Inf4 is shown in red color and the Tyr151 residue of FXIIa is shown as a cyan stick model. (C) A different view of the ribbon and corresponding surface diagram of the model of the Inf4-FXIIa complex. The color scheme is as described in (B). The diagrams are generated by the program UCSF Chimera.

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