1H, 13C and 15N resonance assignments and secondary structures of cyclophilin 2 from Trichomonas vaginalis
Cyclophilins are peptidyl prolyl isomerases that play an important role in a wide variety of biological functions like protein folding and trafficking, intracellular and extracellular signaling pathways, nuclear translocation and in pre-mRNA splicing. Two cyclophilins have been identified in the parasitic organism Trichomonas vaginalis and were named as TvCyP1 and TvCyP2. The 2 enzymes have been found to interact with Myb transcription factors in the parasite which regulate the iron induced expression of ap65-1 gene leading to cytoadherence of the parasite to human vaginal epithelial cells to cause the disease trichomoniasis. TvCyP2 was found to interact specifically with Myb3 to regulate nuclear translocation of the transcription factor. It would be intriguing to identify the binding site of both proteins as it could pave way to newer targets for drug discovery. Here we report the 1H, 13C and 15N resonance assignments and secondary structure information of TvCyP2 that could help us investigate the interaction between Myb3 and TvCyP2 in detail using NMR.
KeywordsTrichomonas vaginalis Peptidyl prolyl isomerases Myb transcription factors Protein secondary structure
The NMR spectra were obtained at the High-field Biomacromolecular NMR Core Facility, Academia Sinica, supported by Core Facilities for Protein Structural Analysis from National Research Program for Biopharmaceuticals (NRPB). This work is supported by Academia Sinica and the Ministry of Science and Technology, Taiwan, ROC (MOST 103-2311-B-001-026-MY3 and MOST 105-2320-B-001-019-MY3).
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