Autor: |
Edisa Rehic, Dana Hoenig, Bianca E. Kamba, Anna Goehring, Eckhard Hofmann, Raphael Gasper, Anja Matena, Peter Bayer |
Jazyk: |
angličtina |
Rok vydání: |
2019 |
Předmět: |
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Zdroj: |
Biomolecules, Vol 9, Iss 3, p 93 (2019) |
Druh dokumentu: |
article |
ISSN: |
2218-273X |
DOI: |
10.3390/biom9030093 |
Popis: |
Trypanosoma 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. |
Databáze: |
Directory of Open Access Journals |
Externí odkaz: |
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