Figure 6.
Fig. 6. A view of the protein backbone for N-TIMP-2
(blue) and the N-MMP-3·TIMP-1 complex (red and white)
showing the differences in structure between the bound and
unbound forms of TIMP at the TIMP/MMP interaction site. The TIMP
structures were superimposed using the coordinates of equivalent
backbone atoms in the -barrel, and
only the N-terminal domain of TIMP-1 is shown. The two zinc ions
of the MMP-3 catalytic domain are shown in magenta (catalytic
site zinc lower left). On the right-hand side of the figure the
AB loop of TIMP-2 can clearly be seen extending far beyond the
TIMP-1 AB loop to make numerous van der Waals clashes with the
N-MMP-3 molecule. The difference in structure of the CD loops
can be seen in the center of the figure. This figure was
produced using MOLMOL (39).
-barrel, and
only the N-terminal domain of TIMP-1 is shown. The two zinc ions
of the MMP-3 catalytic domain are shown in magenta (catalytic
site zinc lower left). On the right-hand side of the figure the
AB loop of TIMP-2 can clearly be seen extending far beyond the
TIMP-1 AB loop to make numerous van der Waals clashes with the
N-MMP-3 molecule. The difference in structure of the CD loops
can be seen in the center of the figure. This figure was
produced using MOLMOL (39).