人类致癌蛋白 NCYM 的 1H、13C 和 15N 主干和侧链共振分配。

IF 0.8 4区 生物学 Q4 BIOPHYSICS Biomolecular NMR Assignments Pub Date : 2024-03-25 DOI:10.1007/s12104-024-10169-3
Assia Mouhand, Kazuma Nakatani, Fumiaki Kono, Yoshitaka Hippo, Tatsuhito Matsuo, Philippe Barthe, Judith Peters, Yusuke Suenaga, Taro Tamada, Christian Roumestand
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引用次数: 0

摘要

NCYM是MYCN癌基因的顺反义基因,编码一种通过抑制GSK3b稳定MYCN的致癌蛋白。NCYM的高表达水平与人类神经母细胞瘤的不良临床预后有关,而在神经母细胞瘤动物模型中,NCYM的过表达会促进远处转移。利用真空-紫外圆二色性和小角 X 射线散射,我们以前曾发现 NCYM 具有部分折叠结构的高度灵活性;然而,要设计出针对 NCYM 的抗癌药物,还需要进一步的结构表征。在此,我们报告了 NCYM 的 1H、15N 和 13C 核磁共振赋值。利用二级化学位移和 TALOS-N 分析进行的二级结构预测表明,NCYM 的结构基本上是无序的,尽管多肽中心区域的残基明显具有采用动态螺旋结构的倾向。这项初步研究为进一步分析 NCYM 与潜在合作伙伴之间的相互作用奠定了基础。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

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1H, 13C and 15N backbone and side-chain resonance assignments of the human oncogenic protein NCYM

NCYM is a cis-antisense gene of MYCN oncogene and encodes an oncogenic protein that stabilizes MYCN via inhibition of GSK3b. High NCYM expression levels are associated with poor clinical outcomes in human neuroblastomas, and NCYM overexpression promotes distant metastasis in animal models of neuroblastoma. Using vacuum-ultraviolet circular dichroism and small-angle X-ray scattering, we previously showed that NCYM has high flexibility with partially folded structures; however, further structural characterization is required for the design of anti-cancer agents targeting NCYM. Here we report the 1H, 15N and 13C nuclear magnetic resonance assignments of NCYM. Secondary structure prediction using Secondary Chemical Shifts and TALOS-N analysis demonstrates that the structure of NCYM is essentially disordered, even though residues in the central region of the peptide clearly present a propensity to adopt a dynamic helical structure. This preliminary study provides foundations for further analysis of interaction between NCYM and potential partners.

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来源期刊
Biomolecular NMR Assignments
Biomolecular NMR Assignments 生物-光谱学
CiteScore
1.70
自引率
11.10%
发文量
59
审稿时长
6-12 weeks
期刊介绍: Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments for proteins and nucleic acids as Assignment Notes. Chemical shifts for NMR-active nuclei in macromolecules contain detailed information on molecular conformation and properties. Publication of resonance assignments in Biomolecular NMR Assignments ensures that these data are deposited into a public database at BioMagResBank (BMRB; http://www.bmrb.wisc.edu/), where they are available to other researchers. Coverage includes proteins and nucleic acids; Assignment Notes are processed for rapid online publication and are published in biannual online editions in June and December.
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