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Figure 6.
FIG. 6. The Hpx domain in pro- and active MMP-1 has a
different conformation. A, both molecules of the asymmetric unit
superimposed on their catalytic domains (dark pink, molecule A;
green, molecule B). Note the difference in Hpx domain
orientation. B, molecule B superimposed with active porcine
MMP-1 (18), superimposed on the catalytic domain (cat). Molecule
B is shown in green; active MMP-1 (Protein Data Bank accession
code 1FBL [PDB]
, porcine MMP-1) is shown in pink. C, same as B but rotated to
show the difference of the catalytic-Hpx domain conformation in
proMMP-1 and active MMP-1. The curved arrow indicates the
relative movement between pro- and active MMP-1. The straight
arrow indicates the cleft between the catalytic domain and the
Hpx domain that is closed in proMMP-1 and open in active MMP-1.
This figure was made with the Swiss-PDB viewer (49).
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