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Updated: Jul 2, 2026

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
Published on: July 16, 2017
Three-dimensional domain architecture of the ADAM family proteinases
1Department of Cardiac Physiology, National Cardiovascular Center Research Institute, 5-7-1 Fujishirodai, Suita, Osaka 565-8565, Japan. stakeda@ri.ncvc.go.jp
Abstract:
A disintegrin and metalloproteinase (ADAM) family of proteins constitutes a major class of mammalian membrane-bound sheddases that are responsible for the processing of cell-surface-protein ectodomains, including the latent forms of growth factors, cytokines and their receptors. However, the molecular mechanism by which ADAMs recognize and process their substrates is largely unknown. Recent crystallographic studies on phylogenically related snake venom metalloproteinases (SVMPs) and mammalian ADAM with thrombospondin type-1 motif (ADAMTS) family proteins have shed light on the structure-function properties of ADAMs. This review will highlight these recent structures, particularly the non-catalytic ancillary domains, which might be important for substrate recognition.
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