Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1941195 | Biochemical and Biophysical Research Communications | 2006 | 8 Pages |
Abstract
Crystal structures of the catalytic domain of human stromelysin-1 (MMP-3) and collagenase-3 (MMP-13) with a hydroxamic acid inhibitor SM-25453 have been solved at 2.01 and 2.37 Å resolutions, respectively. The results revealed that the binding modes for this inhibitor to MMP-3 and -13 were quite similar. However, subtle comparative differences were observed at the bottom of S1′ pockets, which were occupied with the guanidinomethyl moiety of the inhibitor. A remarkable feature of the inhibitor was the deep penetration of its long aliphatic chain into the S1′ pocket and exposure of the guanidinomethyl moiety to the solvent.
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Authors
Tetsuya Kohno, Hitoshi Hochigai, Eiki Yamashita, Tomitake Tsukihara, Masaharu Kanaoka,