A1 Journal article (refereed)
1H, 13C and 15N NMR chemical shift assignments of cAMP-regulated phosphoprotein-19 and -16 (ARPP-19 and ARPP-16) (2020)
Thapa, C. J., Haataja, T., Pentikäinen, U., & Permi, P. (2020). 1H, 13C and 15N NMR chemical shift assignments of cAMP-regulated phosphoprotein-19 and -16 (ARPP-19 and ARPP-16). Biomolecular NMR Assignments, 14(2), 227-231. https://doi.org/10.1007/s12104-020-09951-w
JYU authors or editors
Publication details
All authors or editors: Thapa, Chandan J.; Haataja, Tatu; Pentikäinen, Ulla; Permi, Perttu
Journal or series: Biomolecular NMR Assignments
ISSN: 1874-2718
eISSN: 1874-270X
Publication year: 2020
Volume: 14
Issue number: 2
Pages range: 227-231
Publisher: Springer
Publication country: Netherlands
Publication language: English
DOI: https://doi.org/10.1007/s12104-020-09951-w
Publication open access: Openly available
Publication channel open access: Partially open access channel
Publication is parallel published (JYX): https://jyx.jyu.fi/handle/123456789/69659
Abstract
Protein Phosphatase 2A, PP2A, the principal Serine/threonine phosphatase, has major roles in broad range of signaling pathways that include regulation of cell cycle, cell proliferation and neuronal signaling. The loss of function of PP2A is linked with many human diseases, like cancer and neurodegenerative disorders. Protein phosphatase 2A (PP2A) functions as tumor suppressor and its tumor suppressor activity is inhibited by the overexpression of PP2A inhibitor proteins in most of the cancers. ARPP-19/ARPP-16 has been identified as one of the potential PP2A inhibitor proteins. Here, we report the resonance assignment of backbone 1H, 13C and 15N atoms of human ARPP-19 and ARPP-16 proteins. These chemical shift values can provide valuable information for the further study of the dynamics and interaction of ARPP-proteins to PP2A using NMR spectroscopy.
Keywords: proteins; enzymes; cell signaling; NMR spectroscopy
Free keywords: assignments; cAMP-regulated phosphoprotein-19; HA-detection, intrinsically disordered protein; NMR spectroscopy
Contributing organizations
Related projects
- Conformational properties of intrinsically disordered proteins - biophysical characterization
- Permi, Perttu
- Academy of Finland
Ministry reporting: Yes
Reporting Year: 2020
JUFO rating: 1