理解糖蛋白结构异质性和相互作用：来自天然质谱的见解。
Understanding glycoprotein structural heterogeneity and interactions: Insights from native mass spectrometry.
机构信息
Department of Chemistry, University of Oxford, Oxford, UK; Kavli Institute for Nanoscience Discovery, University of Oxford, Oxford, UK.
Department of Chemistry, University of Oxford, Oxford, UK; Kavli Institute for Nanoscience Discovery, University of Oxford, Oxford, UK.
出版信息
Curr Opin Struct Biol. 2022 Jun;74:102351. doi: 10.1016/j.sbi.2022.102351. Epub 2022 Mar 18.
Protein glycosylation is critical since it connects complex metabolic pathways to diverse proteoforms, fine-tunes protein structures and exerts biological functions. Aberrant glycosylation on the other hand is associated with many diseases, including cancers, inflammation and metabolic disorders. By resolving monosaccharide residues on intact glycoprotein complexes, native mass spectrometry can shed light on glycan heterogeneity, glycoprotein structure and molecular recognition. Here, we focus on the two most prevalent forms of glycosylation, namely N- and O- linked, and discuss recent progress in native mass spectrometry for elucidating glycoprotein structural heterogeneity and relating specific glycan repertoires to glycoprotein interactions.
蛋白质糖基化至关重要，因为它将复杂的代谢途径与多种蛋白质形式联系起来，精细调节蛋白质结构并发挥生物学功能。另一方面，异常的糖基化与许多疾病有关，包括癌症、炎症和代谢紊乱。通过解析完整糖蛋白复合物上的单糖残基，Native MS 可以揭示聚糖异质性、糖蛋白结构和分子识别。在这里，我们重点介绍两种最常见的糖基化形式，即 N-和 O-连接，并讨论 Native MS 阐明糖蛋白结构异质性以及将特定聚糖库与糖蛋白相互作用相关联的最新进展。
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