Figure 1

Structural organization of MMPs, ADAMs and ADAMTS. The typical structure of MMP is made of a prodomain, a furin cleavage site (all MT-MMPs, MMP-21,-23, and -28), a catalytic metalloproteinase domain with fibronectin type II repeats (MMP-2, MMP-9), a linker peptide and a haemopexin domain (except for MMP-7, -26, and -23), a linker peptide, a transmembrane domain and cytoplasmic tail (MMP-14, -15, -16, -24) or glycosylphosphatidylinositol (GPI) anchor (MMP-17, -25). MMP-23 bears C-terminal cysteine-rich (Cys-rich) and Ig-like (Ig) domains and its propeptide lacks a cystein switch motif. Common structure of ADAMs is a prodomain, a cleavage site (by a furin or furin-like proprotein convertase except for ADAM-8 and ADAM-28 which use an autocatalytic process), a metalloproteinase domain, a disintegrin domain, a cysteine-rich region (Cys-rich), an epidermal-growth factor repeat (EGF-like), a transmembrane domain (TM) and a cytoplasmic tail. ADAMTS do not possess a transmembrane domain (TM) but bear a various number of thrombospondin type I motifs (TSP-1) at their C-terminal extremity.