Magdeleine Hung

Matrix metalloproteinase 9 (MMP9) is a member of a large family of proteases that are secreted as inactive zymogens. It is a key regulator of the extracellular matrix, involved in the degradation of various extracellular matrix proteins. MMP9 plays a pathological role in a variety of inflammatory and oncology disorders and has long been considered an attractive therapeutic target.

Author contributions: X.L. and H.J.K. designed the MMP9 construct for crystallization; R.W., M.H. and H.J.K. expressed and purified MMP9 and GS-5745; T.C.A. and A.G.V. crystallized and determined the structure; A.L. performed enzymatic assays; M.H.W. performed binding assays; M.V. and A.E.G. performed the cell culture and tissue experiments; All authors designed experiments and interpreted the results. T.C.A., A.E.G. and H.J.K wrote the paper.