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1H, 13C and 15N NMR chemical shift assignments of cAMP-regulated phosphoprotein-19 and -16 (ARPP-19 and ARPP-16).
Biomolecular NMR Assignments ( IF 0.9 ) Pub Date : 2020-05-28 , DOI: 10.1007/s12104-020-09951-w
Chandan J Thapa 1, 2, 3 , Tatu Haataja 1 , Ulla Pentikäinen 2, 3 , Perttu Permi 1, 4
Affiliation  

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.

中文翻译:

cAMP 调节的磷蛋白-19 和 -16(ARPP-19 和 ARPP-16)的 1H、13C 和 15N NMR 化学位移分配。

蛋白磷酸酶 2A、PP2A 是主要的丝氨酸/苏氨酸磷酸酶,在广泛的信号通路中发挥重要作用,包括调节细胞周期、细胞增殖和神经元信号。PP2A 的功能丧失与许多人类疾病有关,如癌症和神经退行性疾病。蛋白磷酸酶 2A (PP2A) 作为肿瘤抑制因子发挥作用,在大多数癌症中,PP2A 抑制剂蛋白的过度表达会抑制其肿瘤抑制活性。ARPP-19/ARPP-16 已被确定为潜在的 PP2A 抑制剂蛋白之一。在这里,我们报告了主链1 H、13 C 和15的共振分配人类 ARPP-19 和 ARPP-16 蛋白的 N 原子。这些化学位移值可以为使用 NMR 光谱进一步研究 ARPP 蛋白质与 PP2A 的动力学和相互作用提供有价值的信息。
更新日期:2020-05-28
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