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Figure 1.
Fig. 1. Structure of the proMMP-2/TIMP-2 complex. Overall
conformation: the proteinase and inhibitor interact via their
C-terminal domains. The catalytic site of MMP-2 and the
inhibitory active site of TIMP-2 are turned away from each
other. This topology excludes an inhibitory interaction between
the proteinase and inhibitor and implies that both proteins
remain fully functional in the complex. Catalytic and structural
Zn2+ ions are colored red and Ca^2+ ion purple. The  -propeller
blades of the hemopexin domain are numbered from I to IV. Two
light blue ellipsoids in blades III and IV indicate two areas of
interaction between proMMP-2 and TIMP-2 molecules.
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