¹H, 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 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.
Instituto de Bioquímica Médica, CCS, Universidade Federal do Rio de Janeiro, Av. Brigadeiro Trompowiski s/n, Rio de Janeiro, RJ, 21941-590, Brazil.
Rodolpho
R
do Aido-Machado
Didier
D
Salmon
José R
JR
Pires
D002247:Carbon Isotopes; D006859:Hydrogen; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D022061:Tacrolimus Binding Protein 1A / Q000737:chemistry*; D014346:Trypanosoma brucei brucei / Q000201:enzymology*
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D006859:Hydrogen; D022061:Tacrolimus Binding Protein 1A