在SOPH综合征中应用AlphaFold研究NBAS蛋白变异表型。

IF 3.2 4区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Proteins-Structure Function and Bioinformatics Pub Date : 2025-04-01 Epub Date: 2024-12-06 DOI:10.1002/prot.26764
Leonid Zhozhikov, Filipp Vasilev, Nadezhda Maksimova
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引用次数: 0

摘要

NBAS基因变异导致表型不同且不重叠的情况,如SOPH综合征和ILFS2。NBAS是一种所谓的“兼职”蛋白质,负责逆行膜运输和无意义介导的衰变。然而,它的三维模型和它与其他蛋白质可能相互作用的性质仍然难以捉摸。在这里,我们使用AlphaFold预测蛋白-蛋白相互作用(PPI)位点,并将它们映射到NBAS致病变异。我们重复了NBAS蛋白的硅里程碑研究,以解释其变体的多系统表型,特别强调了SOPH变体(p.R1914H)。我们揭示了NBAS主要相互作用伙伴的推定结合位点,并评估了这些结合位点对NBAS蛋白亚结构域结构的影响。利用AlphaFold,我们揭示了NBAS变异对NBAS相关病理患者各表型性状发展的深远影响。
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Protein-Variant-Phenotype Study of NBAS Using AlphaFold in the Aspect of SOPH Syndrome.

NBAS gene variants cause phenotypically distinct and nonoverlapping conditions, SOPH syndrome and ILFS2. NBAS is a so-called "moonlighting" protein responsible for retrograde membrane trafficking and nonsense-mediated decay. However, its three-dimensional model and the nature of its possible interactions with other proteins have remained elusive. Here, we used AlphaFold to predict protein-protein interaction (PPI) sites and mapped them to NBAS pathogenic variants. We repeated in silico milestone studies of the NBAS protein to explain the multisystem phenotype of its variants, with particular emphasis on the SOPH variant (p.R1914H). We revealed the putative binding sites for the main interaction partners of NBAS and assessed the implications of these binding sites for the subdomain architecture of the NBAS protein. Using AlphaFold, we disclosed the far-reaching impact of NBAS variants on the development of each phenotypic trait in patients with NBAS-related pathologies.

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来源期刊
Proteins-Structure Function and Bioinformatics
Proteins-Structure Function and Bioinformatics 生物-生化与分子生物学
CiteScore
5.90
自引率
3.40%
发文量
172
审稿时长
3 months
期刊介绍: PROTEINS : Structure, Function, and Bioinformatics publishes original reports of significant experimental and analytic research in all areas of protein research: structure, function, computation, genetics, and design. The journal encourages reports that present new experimental or computational approaches for interpreting and understanding data from biophysical chemistry, structural studies of proteins and macromolecular assemblies, alterations of protein structure and function engineered through techniques of molecular biology and genetics, functional analyses under physiologic conditions, as well as the interactions of proteins with receptors, nucleic acids, or other specific ligands or substrates. Research in protein and peptide biochemistry directed toward synthesizing or characterizing molecules that simulate aspects of the activity of proteins, or that act as inhibitors of protein function, is also within the scope of PROTEINS. In addition to full-length reports, short communications (usually not more than 4 printed pages) and prediction reports are welcome. Reviews are typically by invitation; authors are encouraged to submit proposed topics for consideration.
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