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Stromelysin-1 also known as matrix metalloproteinase-3 (MMP-3) is an enzyme that in humans is encoded by the MMP3 gene. The MMP3 gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. [5] MMP-3 has an estimated molecular weight of 54 kDa. [6]
X-ray crystallographic structures of several MMP catalytic domains have shown that this domain is an oblate sphere measuring 35 x 30 x 30 Å (3.5 × 3 x 3 nm). The active site is a 20 Å (2 nm) groove that runs across the catalytic domain.
MMP based analysis is an attractive method for computational analysis because they can be algorithmically generated and they make it possible to associate defined structural modifications at the level of compound pairs with chemical property changes, including biological activity. [2] [3] [4]
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Hydroxypyrone-based MMP inhibitors are structurally corresponding to the pyrimidinetriones. A recent inhibitor is the compound 3-hydroxypyran-4-one nominated 868368-30-3. It is MMP-3 selective and its 0,0-bidentate chelation of zinc is the structural part proposed to be responsible for the MMP recognition. [7]
Mutation of the Matrix Metalloproteinase At2-MMP Inhibits Growth and Causes Late Flowering and Early Senescence in Arabidopsis. The Journal of Biological Chemistry, 277 (7) 5541-5547. Graham, J. S., Xiong, J., & Gillikin, J. W. (1991). Purification and developmental Analysis of a Metalloendoproteinase from the Leaves of Glycine max.
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In many instances, the structural protein fold that characterises the clan or family may have lost its catalytic activity, yet retained its function in protein recognition and binding. [citation needed] Metalloproteases are the most diverse of the four main protease types, with more than 50 families classified to date.