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Figure 2.
Figure 2: Specific interactions of calpastatin with calpain
entering and leaving the active-site cleft. a–d, The
27-residue B-peptide^7 is coloured as follows: the residues that
make the loop out of the active site are coloured yellow, the
residues N-terminal to the loop are purple, and the residues
C-terminal to the loop are green. Other calpastatin residues are
coloured dark grey. Hydrogen-bond interactions of calpastatin
with calpain (coloured as in Fig. 1) are shown by black dashed
lines. O and N atoms are coloured red and blue, respectively. a,
Overview of calpain binding at the active site of calpain. b,
Close-up view of the calpastatin at the unprimed side of the
active site. c, Close-up view of calpastatin looping away from
the catalytic residue. d, Close-up view of calpastatin at the
primed side of the active site.
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