全长无配体人Pin1（一种具有结构域间变构作用的磷蛋白调节剂）的主链和侧链化学位移归属
Backbone and side-chain chemical shift assignments of full-length, apo, human Pin1, a phosphoprotein regulator with interdomain allostery.
作者信息
Born Alexandra, Nichols Parker J, Henen Morkos A, Chi Celestine N, Strotz Dean, Bayer Peter, Tate Shin-Ichi, Peng Jeffrey W, Vögeli Beat
机构信息
Department of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus, 12801 East 17th Avenue, Aurora, CO, 80045, USA.
Faculty of Pharmacy, Mansoura University, Mansoura, 35516, Egypt.
出版信息
Biomol NMR Assign. 2019 Apr;13(1):85-89. doi: 10.1007/s12104-018-9857-9. Epub 2018 Oct 23.
Abstract
Pin1 is a human peptidyl-prolyl cis-trans isomerase important for the regulation of phosphoproteins that are implicated in many diseases including cancer and Alzheimer's. Further biophysical study of Pin1 will elucidate the importance of the two-domain system to regulate its own activity. Here, we report near-complete backbone and side-chain H, C and N NMR chemical shift assignments of full-length, apo Pin1 for the purpose of studying interdomain allostery and dynamics.
摘要
Pin1是一种人类肽基脯氨酰顺反异构酶，对磷酸化蛋白的调节很重要，而这些磷酸化蛋白与包括癌症和阿尔茨海默病在内的多种疾病有关。对Pin1进行进一步的生物物理研究将阐明双结构域系统对调节其自身活性的重要性。在此，为了研究结构域间的变构作用和动力学，我们报告了全长无配体Pin1几乎完整的主链和侧链的氢、碳和氮核磁共振化学位移归属。
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