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Natively Inhibited Trypanosoma brucei Cathepsin B Structure Determined by Using an X-ray Laser
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2013 (English)In: Science, ISSN 0036-8075, E-ISSN 1095-9203, Vol. 339, no 6116, 227-230 p.Article in journal (Refereed) Published
Abstract [en]

The Trypanosoma brucei cysteine protease cathepsin B (TbCatB), which is involved in host protein degradation, is a promising target to develop new treatments against sleeping sickness, a fatal disease caused by this protozoan parasite. The structure of the mature, active form of TbCatB has so far not provided sufficient information for the design of a safe and specific drug against T. brucei. By combining two recent innovations, in vivo crystallization and serial femtosecond crystallography, we obtain the room-temperature 2.1 Å resolution structure of the fully glycosylated precursor complex of TbCatB. The structure reveals the mechanism of native TbCatB inhibition and demonstrates that new biomolecular information can be obtained by the "diffraction before destruction" approach of x-ray free-electron lasers from hundreds of thousands of individual microcrystals.

Place, publisher, year, edition, pages
2013. Vol. 339, no 6116, 227-230 p.
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Structural Biology
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URN: urn:nbn:se:uu:diva-189891DOI: 10.1126/science.1229663ISI: 000313328200050PubMedID: 23196907OAI: oai:DiVA.org:uu-189891DiVA: diva2:582543
Available from: 2013-01-04 Created: 2013-01-04 Last updated: 2017-12-06Bibliographically approved

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Seibert, M MarvinCaleman, CarlTimneanu, Nicusor

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