Figure 1.
Figure 1: Overview of calpastatin domain 4 (CAST4) bound to
calpain 2. The overall structure of CAST4 (purple) bound to
the inactive C105S mutant of calpain 2. CAST4, which is
unstructured in the absence of calpain, forms three -helices
when in complex with the enzyme. Helices in subdomains A and C,
which are in contact with DIV (yellow) and DVI (orange), and the
helix in subdomain B, which is in contact with the protease core
DI and DII (blue and light blue, respectively) are shown in
ribbon representation. DIII is coloured green. Gaps in the
electron density of CAST4 are indicated by missing residues
between D589 and K594, and between N629 and P652.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2008,
456,
409-412)
copyright 2008.
-helices
when in complex with the enzyme. Helices in subdomains A and C,
which are in contact with DIV (yellow) and DVI (orange), and the
helix in subdomain B, which is in contact with the protease core
DI and DII (blue and light blue, respectively) are shown in
ribbon representation. DIII is coloured green. Gaps in the
electron density of CAST4 are indicated by missing residues
between D589 and K594, and between N629 and P652.