Structural highlights
Disease
A2ML1_HUMAN Disease susceptibility is associated with variants affecting the gene represented in this entry.
Function
A2ML1_HUMAN Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase (By similarity). Displays inhibitory activity against chymotrypsin, papain, thermolysin, subtilisin A and, to a lesser extent, elastase but not trypsin. May play an important role during desquamation by inhibiting extracellular proteases.[UniProtKB:P01023][1]
References
- ↑ Galliano MF, Toulza E, Gallinaro H, Jonca N, Ishida-Yamamoto A, Serre G, Guerrin M. A novel protease inhibitor of the alpha2-macroglobulin family expressed in the human epidermis. J Biol Chem. 2006 Mar 3;281(9):5780-9. Epub 2005 Nov 18. PMID:16298998 doi:http://dx.doi.org/M508017200
