6533b838fe1ef96bd12a51ee

RESEARCH PRODUCT

1H, 13C and 15N NMR chemical shift assignments of cAMP-regulated phosphoprotein-19 and -16 (ARPP-19 and ARPP-16)

Chandan ThapaChandan ThapaTatu HaatajaPerttu PermiUlla Pentikäinen

subject

entsyymitcAMP-regulated phosphoprotein-19HA-detection intrinsically disordered proteinBiochemistryArticlelaw.inventionSerine03 medical and health sciencesNMR spectroscopy0302 clinical medicineStructural BiologylawAssignmentsNMR-spektroskopiaLoss function030304 developmental biologysoluviestintä0303 health sciencesCell growthChemistryassignmentsProtein phosphatase 2Nuclear magnetic resonance spectroscopyCell cycle3. Good healthCell biologySuppressorproteiinitSignal transduction030217 neurology & neurosurgery

description

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. Electronic supplementary material The online version of this article (doi:10.1007/s12104-020-09951-w) contains supplementary material, which is available to authorized users.

yearjournalcountryeditionlanguage
2020-05-01Biomolecular NMR Assignments
https://doi.org/10.1007/s12104-020-09951-w