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ADAMs (A disintegrin and Metalloproteinases) are major sheddases possessing extracellular metalloproteinase/disintegrin/cysteine-rich (MDC) domains. ADAMs uniquely display both proteolytic and adhesive functions on the cell surface, however, most of their physiological targets and adhesion mechanisms remain unclear. Crystal structures of vascular apotosis-inducing protein- 1 (VAP 1), a snake venom homolog of mammalian ADAMs, reveal ADAMs' MDC domain architecture and a potential target recognition site. The C-shaped structure implies interplay between the ADAMs' proteolytic and adhesive domains and suggests a molecular mechanism for ADAMs' target recognition for shedding.

Crystal Structures of Snake Venom Metalloproteinase and Implication for the Molecular Mechanism of Substrate Recognition by ADAM Family Proteins