A disintegrin & metalloproteinase with thrombospondin type 1 motif 1; ADAMTS-1; ADAM-TS 1; ADAM-TS1; METH-1 (ADAMTS1, KIAA1346, METH1)
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Function
- cleaves aggrecan, a cartilage proteoglycan, & may play role in its turnover (putative)
- cleaves aggrecan at the 1938-Glu-|-Leu-1939 site, within the chondroitin sulfate attachment domain
- has angiogenic inhibitor activity
- active metalloprotease
- may be associated with various inflammatory processes
- may play role in follicular rupture
- precursor is cleaved by a furin endopeptidase
Cofactor: binds 1 Zn+2 per subunit (putative)
Structure
- spacer domain & TSP type-1 domains are important for a tight interaction with the extracellular matrix
- conserved Cys present in the cysteine-switch motif binds the catalytic Zn+2, thus inhibiting the enzyme
- dissociation of Cys from Zn+2 upon activation- peptide release activates the enzyme
- contains 1 disintegrin domain
- contains 1 peptidase M12B domain
- contains 3 TSP type-1 domains
Compartment
Pathology
- may play role in development of cancer cachexia