Structural Analysis of the 42 kDa Parvulin of Trypanosoma brucei
AbstractTrypanosoma brucei is a unicellular eukaryotic parasite, which causes the African sleeping sickness in humans. The recently discovered trypanosomal protein Parvulin 42 (TbPar42) plays a key role in parasite cell proliferation. Homologues of this two-domain protein are exclusively found in protozoa species. TbPar42 exhibits an N-terminal forkhead associated (FHA)-domain and a peptidyl-prolyl-cis/trans-isomerase (PPIase) domain, both connected by a linker. Using NMR and X-ray analysis as well as activity assays, we report on the structures of the single domains of TbPar42, discuss their intra-molecular interplay, and give some initial hints as to potential cellular functions of the protein. View Full-Text
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Rehic, E.; Hoenig, D.; Kamba, B.E.; Goehring, A.; Hofmann, E.; Gasper, R.; Matena, A.; Bayer, P. Structural Analysis of the 42 kDa Parvulin of Trypanosoma brucei. Biomolecules 2019, 9, 93.
Rehic E, Hoenig D, Kamba BE, Goehring A, Hofmann E, Gasper R, Matena A, Bayer P. Structural Analysis of the 42 kDa Parvulin of Trypanosoma brucei. Biomolecules. 2019; 9(3):93.Chicago/Turabian Style
Rehic, Edisa; Hoenig, Dana; Kamba, Bianca E.; Goehring, Anna; Hofmann, Eckhard; Gasper, Raphael; Matena, Anja; Bayer, Peter. 2019. "Structural Analysis of the 42 kDa Parvulin of Trypanosoma brucei." Biomolecules 9, no. 3: 93.
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