Record Details

Title:
Natively inhibited Trypanosoma brucei cathepsin B structure determined by using an X-ray laser
Affiliation(s):
EuXFEL guest, EuXFEL staff
Author group:
Instrument SPB/SFX
Management Board
Keyword(s):
Abstract:
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 obtained the room-temperature 2.1 angstrom 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.
Imprint:
2013
Journal Information:
Science, Vol. 339, p. 227-230, 339<227-230 (2013)
Related external records:
View record in PubMed
DOI: 10.1126/science.1229663
WOS: WOS:000313328200050
WOS: WOS:000313328200050
Language(s):
English


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 Record created 2016-10-11, last modified 2019-02-08

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