The 1H, 15N and 13C backbone resonance assignments of the N-terminal (1-149) domain of Serpine mRNA Binding Protein 1 (SERBP1).

IF 0.8 4区 生物学 Q4 BIOPHYSICS
Antoine Baudin, Hoang H Dinh, Xiaoping Xu, David S Libich
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引用次数: 0

Abstract

Serpine mRNA-Binding Protein 1 (SERBP1) is an RNA-binding protein implicated in diverse cellular functions, including translational regulation, tumor progression, and stress response. It interacts with ribosomal subunits, RNA, and proteins involved in stress granules, contributing to processes such as phase separation and epigenetic regulation. Recent studies have shown SERBP1's role in glioblastoma progression and its involvement in ribosomal regulation. Structurally, SERBP1 contains N- and C-terminal hyaluronan-binding domains, two RG/RGG motifs, and is predicted to be predominantly disordered. Here, we report the backbone resonance assignment and secondary structure propensities of SERBP1's N-terminal residues (1-149). Using NMR spectroscopy, we identified a stable α-helix (residues 28-40) and transient structural elements. These findings provide insight into the structural features of SERBP1 that may mediate its interactions with ribosomal subunits, RNA, and other binding partners, laying a foundation for future structural studies of its functional mechanisms.

丝氨酸mRNA结合蛋白1 (SERBP1) n端(1-149)结构域的1H, 15N和13C骨干共振分配。
丝氨酸mrna结合蛋白1 (SERBP1)是一种与多种细胞功能相关的rna结合蛋白,包括翻译调节、肿瘤进展和应激反应。它与核糖体亚基、RNA和参与应激颗粒的蛋白质相互作用,促进相分离和表观遗传调控等过程。最近的研究表明SERBP1在胶质母细胞瘤进展中的作用及其参与核糖体调节。在结构上,SERBP1包含N端和c端透明质酸结合域,两个RG/RGG基序,预计主要是无序的。在这里,我们报告了SERBP1的n端残基的主共振分配和二级结构倾向(1-149)。通过核磁共振鉴定了一个稳定的α-螺旋(残基28-40)和一个瞬态结构元素。这些发现揭示了SERBP1可能介导其与核糖体亚基、RNA和其他结合伙伴相互作用的结构特征,为未来对其功能机制的结构研究奠定了基础。
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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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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