The selectivity of galardin and an azasugar-based hydroxamate compound for human matrix metalloproteases and bacterial metalloproteases - Fig 1

<p><b>Domain structure of MMPs (A) and schematic representation of galardin and compound 1b (B).</b> All MMPs contain a signal peptide (cleaved off in the endoplasmatic reticulum), a pro-peptide domain and a catalytic domain. In addition, most MMPs contain a linker (hinge-region) and a hemopexin (HPX) like domain. The hinge region in MMP-9 differs from the other MMPs as it is longer and heavily O-glycosylated, and therefore also called the OG-domain. Three secreted (MMP-11, -21, -28) and all membrane-anchored MMPs have a basic RX[K/R]R motif at the C-terminal end of their pro-domain. This motif can be cleaved inside the cells by furin-like proteases. The two gelatinases (MMP-2, -9) contain three fibronectin II like repeats (FnII module) in their catalytic domain, located N-terminal to the catalytic Zinc-binding site. Four of the six membrane-type (MT)-MMPs are anchored to the cell membranes through a type I transmembrane domain and the other two through a glycosylphosphatidylinosityl (GPI) moiety.