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本文引用的文献

1
Hydrogen/deuterium exchange memory NMR reveals structural epitopes involved in IgE cross-reactivity of allergenic lipid transfer proteins.氢/氘交换记忆 NMR 揭示了变应原脂质转移蛋白 IgE 交叉反应涉及的结构表位。
J Biol Chem. 2020 Dec 18;295(51):17398-17410. doi: 10.1074/jbc.RA120.014243.
2
Physical Principles Underlying the Complex Biology of Intracellular Phase Transitions.细胞内相转变的复杂生物学的物理原理。
Annu Rev Biophys. 2020 May 6;49:107-133. doi: 10.1146/annurev-biophys-121219-081629. Epub 2020 Jan 31.
3
Blind tests of RNA-protein binding affinity prediction.RNA-蛋白质结合亲和力预测的盲测。
Proc Natl Acad Sci U S A. 2019 Apr 23;116(17):8336-8341. doi: 10.1073/pnas.1819047116. Epub 2019 Apr 8.
4
An NMR View of Protein Dynamics in Health and Disease.NMR 视角下的健康与疾病中的蛋白质动力学。
Annu Rev Biophys. 2019 May 6;48:297-319. doi: 10.1146/annurev-biophys-052118-115647. Epub 2019 Mar 22.
5
The clinical relevance of lipid transfer protein.脂质转移蛋白的临床相关性。
Clin Exp Allergy. 2018 Jan;48(1):6-12. doi: 10.1111/cea.13053. Epub 2017 Dec 1.
6
Using chemical shift perturbation to characterise ligand binding.利用化学位移扰动来表征配体结合。
Prog Nucl Magn Reson Spectrosc. 2013 Aug;73:1-16. doi: 10.1016/j.pnmrs.2013.02.001. Epub 2013 Mar 21.
7
IgE and mast cells in allergic disease.变应性疾病中的 IgE 和肥大细胞。
Nat Med. 2012 May 4;18(5):693-704. doi: 10.1038/nm.2755.
8
Differential hydrogen/deuterium exchange mass spectrometry analysis of protein-ligand interactions.蛋白质-配体相互作用的差分式氢/氘交换质谱分析。
Expert Rev Proteomics. 2011 Feb;8(1):43-59. doi: 10.1586/epr.10.109.
9
Structure and intermolecular dynamics of aggregates populated during amyloid fibril formation studied by hydrogen/deuterium exchange.通过氢/氘交换研究淀粉样纤维形成过程中聚集物的结构和分子间动力学。
Acc Chem Res. 2010 Aug 17;43(8):1072-9. doi: 10.1021/ar9002784.
10
Hydrogen exchange and structural dynamics of proteins and nucleic acids.蛋白质和核酸的氢交换与结构动力学
Q Rev Biophys. 1983 Nov;16(4):521-655. doi: 10.1017/s0033583500005217.

通过 NMR 光谱技术绘制不可见表位图谱。

Mapping invisible epitopes by NMR spectroscopy.

机构信息

Department of Biochemistry and Molecular Biology and Center for Eukaryotic Gene Regulation, Pennsylvania State University, University Park, Pennsylvania, USA.

Department of Biochemistry and Molecular Biology and Center for Eukaryotic Gene Regulation, Pennsylvania State University, University Park, Pennsylvania, USA; Department of Chemistry, Pennsylvania State University, University Park, Pennsylvania, USA.

出版信息

J Biol Chem. 2020 Dec 18;295(51):17411-17412. doi: 10.1074/jbc.H120.016607.

DOI:10.1074/jbc.H120.016607
PMID:33453987
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7762964/
Abstract

Defining discontinuous antigenic epitopes remains a substantial challenge, as exemplified by the case of lipid transfer polyproteins, which are common pollen allergens. Hydrogen/deuterium exchange monitored by NMR can be used to map epitopes onto folded protein surfaces, but only if the complex rapidly dissociates. Modifying the standard NMR-exchange measurement to detect substoichiometric complexes overcomes this time scale limitation and provides new insights into recognition of lipid transfer polyprotein by antibodies. In the future, this new and exciting development should see broad application to a range of tight macromolecular interactions.

摘要

定义不连续的抗原表位仍然是一个巨大的挑战,脂质转移多蛋白就是一个很好的例子,它是常见的花粉过敏原。通过 NMR 监测的氢/氘交换可用于将表位映射到折叠蛋白质表面,但前提是该复合物快速解离。通过修改标准的 NMR 交换测量来检测亚化学计量复合物,克服了这个时间尺度限制,并为抗体识别脂质转移多蛋白提供了新的见解。在未来,这一新的令人兴奋的发展应该会广泛应用于一系列紧密的大分子相互作用。