H, ¹⁵N and ¹³C assignments of a putative peptidyl prolyl cis-trans isomerase FKBP12 from Trypanosoma brucei

TbFKBP12 is a putative peptidyl prolyl cis-trans isomerase from Trypanosoma brucei, causative agent of the African trypanosomiasis or sleeping sickness. It interacts with the immunosuppressive drug rapamycin inhibiting the formation of TORC2 complex leading to parasite death by inhibiting cell proli...

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Bibliographic Details
Published in:Biomolecular NMR assignments 2014-04, Vol.8 (1), p.133-135
Main Authors: do Aido-Machado, Rodolpho, Salmon, Didier, Pires, José R
Format: Article
Language:English
Subjects:
Carbon Isotopes
Hydrogen
Nitrogen Isotopes
Nuclear Magnetic Resonance, Biomolecular
Protein Structure, Secondary
Tacrolimus Binding Protein 1A - chemistry
Trypanosoma brucei brucei - enzymology
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Summary:TbFKBP12 is a putative peptidyl prolyl cis-trans isomerase from Trypanosoma brucei, causative agent of the African trypanosomiasis or sleeping sickness. It interacts with the immunosuppressive drug rapamycin inhibiting the formation of TORC2 complex leading to parasite death by inhibiting cell proliferation through cytokinesis blockade. Moreover, RNAi silencing of TbFKBP12 revealed essential function in both procyclic and bloodstream forms. Both facts make TbFKBP12 an attractive target for ligand development and thus structural data is desirable. In this work we report the NMR resonance assignments for (1)H, (15)N and (13)C nuclei in the backbone and side chains of the TbFKBP12 as basis for further studies of structure, backbone dynamics, interaction mapping and drug screening.
ISSN:1874-270X
DOI:10.1007/s12104-013-9468-4