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Figure 3.
Figure 3. (a) Surface representation of the model of the
complex TF (green), fVIIa (catalytic domain in pink and EGF1,
EGF2 and Gla domains in yellow), fX (catalytic domain in gray
and EGF1, EGF2 and Gla domains in blue). NAPc2 is in red (ribbon
representation), yellow circle and arrow indicate the position
of the insertion-loop containing the P1 (Arg44) residue. (b)
Same as (a) but with the fXa re-positioned to permit the
simultaneous binding of NAPc2 to the fXa exosite and the fVIIa
active site. (c) Ribbon representation of the fXa-NAPc2 complex.
The yellow circle indicates the antiparallel β-strand
interactions between NAPc2 (red) and fXa (dark blue). (d)
Surface charge of fVIIa with the modeled peptide fragment of the
NAPc2 insertion-loop containing Arg44 in the active site
cavity. Figure 3. (a) Surface representation of the model of
the complex TF (green), fVIIa (catalytic domain in pink and
EGF1, EGF2 and Gla domains in yellow), fX (catalytic domain in
gray and EGF1, EGF2 and Gla domains in blue). NAPc2 is in red
(ribbon representation), yellow circle and arrow indicate the
position of the insertion-loop containing the P1 (Arg44)
residue. (b) Same as (a) but with the fXa re-positioned to
permit the simultaneous binding of NAPc2 to the fXa exosite and
the fVIIa active site. (c) Ribbon representation of the
fXa-NAPc2 complex. The yellow circle indicates the antiparallel
β-strand interactions between NAPc2 (red) and fXa (dark blue).
(d) Surface charge of fVIIa with the modeled peptide fragment of
the NAPc2 insertion-loop containing Arg44 in the active site
cavity.
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