總結(jié) |
The superfamily of high molecular weight serine proteinaseinhibitors (serpins) regulate a diverse set of intracellular andextracellular processes such as complement activation,fibrinolysis, coagulation, cellular differentiation, tumorsuppression, apoptosis, and cell migration. Serpins arecharacterized by well-conserved a tertiary structure that consistsof 3 beta sheets and 8 or 9 alpha helices (Huber and Carrell, 1989[PubMed 2690952]). A critical portion of the molecule, the reactivecenter loop connects beta sheets A and C. Protease inhibitor-8(PI8; SERPINB8) is a member of the ov-serpin subfamily, which,relative to the archetypal serpin PI1 (MIM 107400), ischaracterized by a high degree of homology to chicken ovalbumin,lack of N- and C-terminal extensions, absence of a signal peptide,and a serine rather than an asparagine residue at the penultimateposition (summary by Bartuski et al., 1997 [PubMed9268635]).
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