Figure 1
Figure 1. Spatial localization of the mutations in mFVIIa-VEAY (VEAY) and mFVIIa-DVQ (DVQ) on the heavy chain compared with mFVII wild-type (WT). The crystal structure of the heavy chain of human FVIIa (1DAN31) was used as a template for homology modeling (see “Statistical analysis and protein percentage identity calculation and homology-based modeling”). The catalytic triad (CT, orange [His193, Asp242, Ser194]) and the location of the newly formed N-terminus of the heavy chain of the activated form are shown (Ile153, yellow). The VEAY mutations are: Leu305Val (green); Ala314Glu (red); Lys337Ala (white); Ile374Tyr (magenta). The DVQ mutations are: Val158Asp (red); Glu296Val (green); Met298Gln (purple). Amino acid numbering refers to the mature secreted mFVII.

Spatial localization of the mutations in mFVIIa-VEAY (VEAY) and mFVIIa-DVQ (DVQ) on the heavy chain compared with mFVII wild-type (WT). The crystal structure of the heavy chain of human FVIIa (1DAN31 ) was used as a template for homology modeling (see “Statistical analysis and protein percentage identity calculation and homology-based modeling”). The catalytic triad (CT, orange [His193, Asp242, Ser194]) and the location of the newly formed N-terminus of the heavy chain of the activated form are shown (Ile153, yellow). The VEAY mutations are: Leu305Val (green); Ala314Glu (red); Lys337Ala (white); Ile374Tyr (magenta). The DVQ mutations are: Val158Asp (red); Glu296Val (green); Met298Gln (purple). Amino acid numbering refers to the mature secreted mFVII.

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