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Structure, interdomain dynamics and pH-dependent autoactivation of pro-rhodesain, the main lysosomal cysteine protease from African trypanosomes
Patrick Johé, Elmar Jaenicke, View ORCID ProfileHannes Neuweiler, View ORCID ProfileTanja Schirmeister, View ORCID ProfileChristian Kersten, View ORCID ProfileUte A. Hellmich
doi: https://doi.org/10.1101/2020.11.10.363747
Patrick Johé
1Institute of Pharmaceutical and Biomedical Sciences, Johannes Gutenberg-University, Mainz, Germany
Elmar Jaenicke
3Institute for Molecular Physiology, Johannes Gutenberg-University, Mainz, Germany
Hannes Neuweiler
2Department for Biotechnology and Biophysics, Julius-Maximilians-University, Würzburg, Germany
Tanja Schirmeister
1Institute of Pharmaceutical and Biomedical Sciences, Johannes Gutenberg-University, Mainz, Germany
Christian Kersten
1Institute of Pharmaceutical and Biomedical Sciences, Johannes Gutenberg-University, Mainz, Germany
Ute A. Hellmich
4Department Chemistry, Biochemistry Division, Johannes Gutenberg-University, Mainz, Germany
5Centre for Biomolecular Magnetic Resonance (BMRZ), Goethe University, Frankfurt, Germany
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Posted November 10, 2020.
Structure, interdomain dynamics and pH-dependent autoactivation of pro-rhodesain, the main lysosomal cysteine protease from African trypanosomes
Patrick Johé, Elmar Jaenicke, Hannes Neuweiler, Tanja Schirmeister, Christian Kersten, Ute A. Hellmich
bioRxiv 2020.11.10.363747; doi: https://doi.org/10.1101/2020.11.10.363747
Structure, interdomain dynamics and pH-dependent autoactivation of pro-rhodesain, the main lysosomal cysteine protease from African trypanosomes
Patrick Johé, Elmar Jaenicke, Hannes Neuweiler, Tanja Schirmeister, Christian Kersten, Ute A. Hellmich
bioRxiv 2020.11.10.363747; doi: https://doi.org/10.1101/2020.11.10.363747
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