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The specificity of proteasomes: impact on MHC class I processing and presentation of antigens
- G. Niedermann, E. Geier, M. Lucchiari-Hartz, N. Hitziger, A. Ramsperger, K. Eichmann
- BiologyImmunological reviews
- 1 December 1999
It is found that polypeptide processing is remarkably conserved among proteasomes of enkaryotic origin and that invertebrate proteasome can efficiently produce known high‐copy MHC class I ligands, suggesting evolutionary adaptation of the transporter associated with antigen processing and MHCclass I to ancient constraints imposed by proteasomal protein’ degradation.
Evolution of vitamin B2 biosynthesis. A novel class of riboflavin synthase in Archaea.
Crystal Structure of an Archaeal Pentameric Riboflavin Synthase in Complex with a Substrate Analog Inhibitor
- A. Ramsperger, M. Augustin, M. Fischer
- Chemistry, BiologyJournal of Biological Chemistry
- 13 January 2006
The topology of the two bound ligands at the active site is well in line with the known stereochemistry of a pentacyclic adduct of 6,7-dimethyl-8-ribityllumazine that has been shown to serve as a kinetically competent intermediate of trimeric and pentameric riboflavin synthases.
Crystal Structure of an archaeal pentameric riboflavin synthase