1H, 13C, and 15N resonance assignments of human glutathione peroxidase 4
1H, 13C, and 15N resonance assignments of human glutathione peroxidase 4
复制标题
人谷胱甘肽过氧化物酶 4 的 1H、13C 和 15N 共振分配
DOI：
10.1007/s12104-022-10090-7
复制
发表时间：
2022
影响因子：
0.9
通讯作者：
Kojima Chojiro
中科院分区：
文献类型：
--
作者：
Furuita Kyoko;Inomata Kouki;Sugiki Toshihiko;Kobayashi Naohiro;Fujiwara Toshimich;Kojima Chojiro
谷胱甘肽过氧化物酶 4 (GPx4) 是一种抗氧化酶，能够直接还原细胞膜内的过氧化磷脂。最近，GPx4作为癌症治疗的靶分子引起了人们的关注，因为它可以诱导癌细胞永生化，抑制铁死亡。在本研究中，为了通过溶液NMR分析GPx4的功能和结构，我们对GPx4进行了共振归属，并归属了几乎所有主链1H、13C和15N共振以及大部分侧链1H和13C共振。利用这些分配，通过 TALOS + 程序分析 GPx4 的二级结构。 GPx4 有六个螺旋和七个链。然后，通过 {1H}–15N 异核 NOE 实验检查主链动力学。发现 GPx4 除了短环区域外都是刚性的。这些结果将为GPx4的功能分析和首次溶液结构确定提供依据。
Glutathione peroxidase 4 (GPx4) behaves as an antioxidant enzyme capable of directly reducing peroxidized phospholipids within cell membranes. Recently, GPx4 has attracted attention as a target molecule for cancer therapy because it induces the immortalization of cancer cells suppressing ferroptosis. In this study, to analyze the function and structure of GPx4 by solution NMR, we performed resonance assignments of GPx4 and assigned almost all backbone1H,13C, and15N resonances and most of the side chain1H and13C resonances. Using these assignments, the secondary structure of GPx4 was analyzed by the TALOS + program. GPx4 has six helices and seven strands. Then, the backbone dynamics were examined by the {1H}–15N heteronuclear NOE experiment. GPx4 was found to be rigid except for a short loop region. These results will provide basis for functional analysis and the first solution structure determination of GPx4.