小鼠NOTCH1 EGF27的1H, 15N, 13C骨干和侧链共振分配和二级结构

IF 0.8 4区 生物学 Q4 BIOPHYSICS Biomolecular NMR Assignments Pub Date : 2022-12-24 DOI:10.1007/s12104-022-10116-0
Justin A. Grennell, Kendra D. Jenkins, Kelvin B. Luther, John Glushka, Robert S. Haltiwanger, Megan A. Macnaughtan
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引用次数: 0

摘要

NOTCH1是后生动物中的一种跨膜受体,与多种疾病有关。该受体包含一个细胞外结构域(ECD),具有36个串联表皮生长因子样(EGF)重复序列。ECD通过与邻近细胞的蛋白质配体相互作用负责细胞间信号传导。每个EGF重复序列由大约40个氨基酸和3个保守的二硫键组成。Abruptex区域(EGF24-29)对NOTCH1信号传导至关重要,并以其错义突变而闻名。某些EGF重复序列通过添加o链聚糖进行修饰,并且许多具有钙结合位点,这使每个EGF重复序列具有独特的功能。研究表明,EGF27 O-聚焦位点的缺失会改变NOTCH1的活性。为了研究糖基化在NOTCH1信号通路中的作用,我们利用核磁共振波谱技术研究了EGF27及其糖型的结构。在这里,我们报告了未修饰的EGF27蛋白的主链和侧链1H, 15N和13c共振分配以及由分配的化学位移得出的预测二级结构。
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1H, 15N, 13C backbone and sidechain resonance assignments and secondary structure of mouse NOTCH1 EGF27

NOTCH1 is a transmembrane receptor in metazoans that is linked to a variety of disorders. The receptor contains an extracellular domain (ECD) with 36 tandem epidermal growth factor-like (EGF) repeats. The ECD is responsible for intercellular signaling via protein–ligand interactions with neighboring cells. Each EGF repeat consists of approximately 40 amino acids and 3 conserved disulfide bonds. The Abruptex region (EGF24-29) is critical for NOTCH1 signaling and is known for its missense mutations. Certain EGF repeats are modified with the addition of O-linked glycans and many have calcium binding sites, which give each EGF repeat a unique function. It has been shown that the loss of the O-fucose site of EGF27 alters NOTCH1 activity. To investigate the role of glycosylation in the NOTCH1 signaling pathway, nuclear magnetic resonance spectroscopy has been employed to study the structures of EGF27 and its glycoforms. Here, we report the backbone and sidechain 1H, 15N, and 13C-resonance assignments of the unmodified EGF27 protein and the predicted secondary structure derived from the assigned chemical shifts.

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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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