In this acclaimed thesis, Eva Maria Huber reveals ground-breaking results by elucidating the crystal structure of the murine immunoproteasome in complex with a selective inhibitor. Huber does this by performing multidisciplinary methodologies including X-ray crystallography, fluorescence spectroscopy and mutagenesis experiments. Her exceptional results explore the immunoproteasome complex structures and are of outstanding importance for future scientific research especially in the pharmaceutical industry. These results will enable the functional analysis of individual proteasome subunits and support the development of novel drugs for autoimmune diseases such as multiple sclerosis or rheumatoid arthritis.

Introduction.- Objective.- Materials and Methods.- Results.- Discussion.- Appendix.

Eva Huber studied biochemistry at the Technische Universität München (TUM) from 2004 till 2009. For her master studies, which were funded by the Studienstiftung des deutschen Volkes, she received the Jürgen-Manchot Studienpreis from the faculty of chemistry of the TUM. During her postgraduate studies (2009-2013) in the group of Prof. Groll at the TUM she succeeded in the elucidation of the mouse immuno- and constitutive proteasome X-ray structures in their unliganded state and in complex with the immunoproteasome-selective compound ONX 0914. For these results she has been awarded the "Management Engineers Presidential Award" in 2012.