A1 Refereed original research article in a scientific journal
1H, 13C and 15N NMR chemical shift assignments of cAMP-regulated phosphoprotein-19 and -16 (ARPP-19 and ARPP-16)
Authors: Chandan J. Thapa, Tatu Haataja, Ulla Pentikäinen, Perttu Permi
Publisher: Springer
Publication year: 2020
Journal: Biomolecular NMR Assignments
Journal name in source: Biomolecular NMR Assignments
Volume: 14
Issue: 2
Number of pages: 5
ISSN: 1874-2718
DOI: https://doi.org/10.1007/s12104-020-09951-w
Self-archived copy’s web address: https://research.utu.fi/converis/portal/detail/Publication/48590459
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.
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