cd02056: alpha-1-antitrypsin_like (this model, PSSM-Id:239011 is obsolete and has been replaced by 381012)
alpha-1-antitrypsin_like. This family contains a variety of different members of clade A of the serpin superfamily. They include the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and noninhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia.
Structure:1QLP_A; active conformation-loop out; P1-P1' cleavage site: Met-Ser. - View structure with Cn3D
Comment:depending on the conformational state, the RC loop is surface accessible in the active form or buried and inserted as the central beta strand in the inactive form.
Jiyao W et al.(2023). "The conserved domain database in 2023.",