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Biomolecular NMR Assignments

, Volume 13, Issue 1, pp 239–243 | Cite as

Backbone and side chain 1H, 15N and 13C assignments of a putative peptidyl prolyl cis–trans isomerase FKBP12 from Mycobacterium tuberculosis

  • Guilherme Caldas Andrade
  • Luis Felipe Correa Silva
  • Danielle Maria Perpétua Oliveira
  • José Ricardo M. Pires
  • Fabio C. L. AlmeidaEmail author
  • Cristiane Dinis AnobomEmail author
Article

Abstract

FK506 Binding Proteins (FKBPs) are a family of highly conserved and important proteins that possess a peptidyl cis–trans isomerase (PPIases) domain. Human FKBP12 is a prototype of this family and it is involved in many diseases due to its interaction with the immunosuppressive drugs FK506 and rapamycin. They inhibit calcineurin and mTOR complex, respectively, leading to parasite death by inhibiting cell proliferation through cytokinesis blockade being an important target to find new drugs. Tuberculosis is a disease that causes important impacts on public health worldwide. In this context, MtFKBP12 is a putative peptidyl prolyl cis–trans isomerase from Mycobacterium tuberculosis and here we report the NMR chemical shift assignment for 1H, 15N and 13C nuclei in the backbone and side chains of the MtFKBP12. This lays the foundation for further structural studies, backbone dynamics, mapping of interactions and drug screening and development. We have found through the NMR spectrum that the protein is well folded with narrow peaks and almost none overlap in 15N-HSQC. Prediction of secondary structure using Talos-N server showed great similarity with other proteins from this family.

Keywords

FKBP Mycobacterium tuberculosis NMR Assignment 

Notes

Acknowledgements

This work was funded by FAPERJ Grants 239229 and 204432, awarded to FCLA, CNPq Grant 309564/2017-4, awarded to FCLA. We also thank to INBEB-INCT for funding. The assignment was deposit at the Biomagnetic Resonance Data Bank (BMRB ID 27690). GCA is funded by CAPES scholarship and LFCS is funded by FAPERJ.

Compliance with ethical standards

Conflict of interest

The authors declare no conflict of interest.

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Copyright information

© Springer Nature B.V. 2019

Authors and Affiliations

  1. 1.Institute of ChemistryFederal University of Rio de JaneiroRio de JaneiroBrazil
  2. 2.Institute of Medical Biochemistry (IBqM), National Center of Nuclear Magnetic Resonance Jiri JonasFederal University of Rio de JaneiroRio de JaneiroBrazil
  3. 3.National Center of Nuclear Magnetic Resonance (CNRMN), Center for Structural Biology and Bioimaging (CENABIO)Federal University of Rio de JaneiroRio de JaneiroBrazil

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