The
immunoproteasome breaks proteins into peptides that are then presented on the cellular surface. The
immune system can distinguish between self and nonself peptides and selectively kills cells that due to a
viral infection present non-self peptides at their surface. In
autoimmune diseases this mechanism is deregulated and the immune system also eliminates uninfected cells by mistake. However, inhibition of the immunoproteasome may alleviate disease symptoms and progression. Biochemists at the Technische Universitaet Muenchen (TUM) now succeeded in determining the first crystal structure of an immunoproteasome. The results are reported in the renowned journal
Cell and will enable the development of new drugs that selectively target the immunoproteasome.
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