|
Figure 1.
Figure 1. Stereo views of the cdMMP-13/TIMP-2 complex (blue
ribbon, catalytic domain; orange ribbon, TIMP-2), optimally
overlaid with the formerly determined cdMMP-14/TIMP-2 complex
(grey rope, catalytic domain; green rope, TIMP-2).^25 Helices,
strands and selected loops of the cdMMP-13/TIMP2 complex are
labelled. Due to their more similar conformation, essentially
both catalytic domains are superimposed. The MMP-13 catalytic
domain differs in that the N-terminal segment nestles against
the proteinase surface, forming a surface-located salt-bridge,
and by lacking the characteristic MT-loop. (a) Front view. (b)
Side view. Figure 1. Stereo views of the cdMMP-13/TIMP-2
complex (blue ribbon, catalytic domain; orange ribbon, TIMP-2),
optimally overlaid with the formerly determined cdMMP-14/TIMP-2
complex (grey rope, catalytic domain; green rope, TIMP-2).[3]^25
Helices, strands and selected loops of the cdMMP-13/TIMP2
complex are labelled. Due to their more similar conformation,
essentially both catalytic domains are superimposed. The MMP-13
catalytic domain differs in that the N-terminal segment nestles
against the proteinase surface, forming a surface-located
salt-bridge, and by lacking the characteristic MT-loop. (a)
Front view. (b) Side view.
|
