Alpha-2-macroglobulin/Complement system
IPR050473
Definition
The alpha-2-macroglobulin family includes protease inhibitors that use a unique 'trapping' mechanism to inhibit all four classes of proteinases. Members contain a bait region with specific cleavage sites for different proteinases. Upon cleavage, a conformational change traps the proteinase, reducing its activity against high molecular weight substrates while remaining active against smaller substrates. A thioester bond is hydrolyzed post-cleavage, allowing covalent binding to the proteinase. Some family members play roles in the immune response by binding pathogens and mediating clearance through lysis or melanization. Others are involved in the complement system, acting as non-enzymatic components of C3 and C5 convertases, or as mediators of local inflammatory processes. The family also includes complement components that are central to the complement system activation and function in chronic inflammation as chemoattractants for neutrophils.
11 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
Loading the interactive Seroatlas explorer...