Department of Molecular Biology and Biophysics, UConn Health, 263 Farmington Avenue, Farmington, CT, 06032, USA.
Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA, USA.
Biomol NMR Assign. 2022 Oct;16(2):197-203. doi: 10.1007/s12104-022-10079-2. Epub 2022 May 10.
Ubiquitin specific protease 7 (USP7) is a deubiquitinating enzyme, which removes ubiquitin tag from numerous protein substrates involved in diverse cellular processes such as cell cycle regulation, apoptosis and DNA damage response. USP7 affects stability, interaction network and cellular localization of its cellular and viral substrates by controlling their ubiquitination status. The large 41 kDa catalytic domain of USP7 harbors the active site of the enzyme. Here we present a nearly complete (93%) NMR resonance assignment of isoleucine, leucine and valine (ILV) side-chains of the USP7 catalytic domain along with a refined nearly complete (93%) assignment of its backbone resonances. The reported ILV methyl group assignment will facilitate further NMR investigations of structure, interactions and conformational dynamics of the USP7 enzyme.
泛素特异性蛋白酶 7（USP7）是一种去泛素化酶，可去除参与多种细胞过程的众多蛋白质底物上的泛素标签，如细胞周期调控、细胞凋亡和 DNA 损伤反应。USP7 通过控制其底物的泛素化状态来影响细胞和病毒底物的稳定性、相互作用网络和细胞定位。USP7 的大型 41 kDa 催化结构域包含酶的活性位点。在这里，我们提供了 USP7 催化结构域中异亮氨酸、亮氨酸和缬氨酸（ILV）侧链的近完整（93%）NMR 共振分配，以及其骨架共振的近乎完整（93%）分配。报告的 ILV 甲基组分配将有助于进一步研究 USP7 酶的结构、相互作用和构象动力学。
