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Figure 1.
Figure 1: Crystallographic structures of active, latent and
self-terminating dimer of the serpin antithrombin. a, Active
antithrombin is shown with the RCL on top (yellow) and the  -sheet
A facing (red, with numbered strands). Either by proteolytic
cleavage in the RCL or by extraction of strand 1C (s1C, orange),
serpins incorporate the RCL into -sheet
A as strand 4A (s4A) resulting in a hyperstable six-stranded
conformation. Polymerogenic mutations are shown (yellow is Z,
magenta is Mmalton, blue is Siiyama and Syracuse, red and cyan
are His338Arg and Gly392Glu neuroserpin^3, and green is P80S
antithrombin^11). The loop connecting strand 6A to 5A is in
cyan. b, The latent conformer of antithrombin is shown coloured
as in a. Residues on strands 5 and 6A, which were mutated to Cys
(see Fig. 2a), are indicated by green balls. c, The structure of
the stable antithrombin dimer (monomer A coloured as in b, and
monomer B is pale green).
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