Protease as adhesion molecule-enzyme

ADAMs focused on the function of the disintegrin domain in cell‐cell and  cell‐matrix interactions. An example is the analysis of the crystal structure of the mature ADAM-22 ectodomain, one of the catalytically inactive ADAMs. In this analysis, ADAM-22 displays a four-leafed clover structure of four domains, the MDCE without the pro-domain. According to this, the authors proposed that ADAMs function is modulated by dynamic structural changes in M domain and DCE domains that allow for the opening and closing of the protein configuration. Electron microscopy studies on the full-length ADAM-12-s showed a similar four-leafed structure. In this structure, as for ADAM-22, the pro-domain is an integral domain of mature ADAM12 non-covalently associated to M domain.

In addition to mediating interactions with cell surface receptors for adhesive and fusogenic purposes, the disintegrin and cysteine domains were suggested to regulate the proteolytic function of ADAMs as shown for the shedding of interleukin-1 receptor-II by ADAM-17.

ADAMs (A Disintegrin and Metalloprotease)

ADAMTSs (ADAM metalloprotease with ThromboSpondin type 1 motif)