Figure 3.
Figure 3: Models of the serpin polymer and the M* state. a, A
model of a linear serpin dimer (coloured as in Fig. 1c), with
balls indicating AspN cleavage sites found in polymers of
antithrombin (magenta) and [1]AT
(cyan). The yellow ball shows the position of the Leu303Cys
substitution (Fig. 2c). b, A modelled pentamer was formed by the
addition of protomers to both ends of the dimer. c, A model of
the polymerogenic folding intermediate (M*) with the contiguous
loop from the C terminus of strand 6A to strand 1C in a
random-coil conformation. New proteolytic sites in this region
(magenta balls for antithrombin, cyan balls for [1]AT
and green balls for PAI-1; ref. 20) were detected for the M*
state (Fig. 2d).
[1]AT
(cyan). The yellow ball shows the position of the Leu303Cys
substitution (Fig. 2c). b, A modelled pentamer was formed by the
addition of protomers to both ends of the dimer. c, A model of
the polymerogenic folding intermediate (M*) with the contiguous
loop from the C terminus of strand 6A to strand 1C in a
random-coil conformation. New proteolytic sites in this region
(magenta balls for antithrombin, cyan balls for