A molecular basis for glycosylation-induced conformational switching.
A molecular basis for glycosylation-induced conformational switching.
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DOI：
10.1016/s1074-5521(98)90159-4
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发表时间：
1998-08
影响因子：
--
通讯作者：
Sarah E. O'Connor;Barbara Imperiali
中科院分区：
文献类型：
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作者：
Sarah E. O'Connor;Barbara Imperiali
背景：天冬酰胺连接的糖基化对糖蛋白的结构和功能有很大的影响。然而，在大多数情况下，目前还不清楚具体如何与蛋白质的碳水化合物部分相互作用，以影响其conformation.Results：一系列的糖肽的基础上的关键A285糖基化位点的血凝素糖蛋白从流感病毒被用作模型系统来研究天冬酰胺连接的糖基化的影响。这种肽与一个家庭的短碳水化合物的衍生化表明，在碳水化合物的结构的微妙变化有显着的影响肽构象。用截短形式的天然碳水化合物修饰血凝素糖肽诱导与天然蛋白质中发现的结构相似的β-转角结构。结论：N-乙酰基可能通过与肽的空间位阻作用，促进肽的β-转角构象变得更加紧密。这项研究表明，碳水化合物组成的相对较小的变化可以对糖肽构象产生显着的影响。
Background:Asparagine-linked glycosylation has the capacity to greatly influence the structure and function of glycoproteins. In most cases, however, it is unclear specifically how the carbohydrate moiety interacts with the protein to influence its conformation.Results:A series of glycopeptides based on the critical A285 glycosylation site of the hemagglutinin glycoprotein from influenza virus was used as a model system to study the effects of asparagine-linked glycosylation. Derivatization of this peptide with a family of short carbohydrates reveals that subtle changes in the structure of the carbohydrate have a dramatic impact on peptide conformation. Modification of the hemagglutinin glycopeptide with a truncated version of the native carbohydrate induces a β-turn structure similar to the structure found in the native protein. Replacement of the C2 and C2′N-acetyl groups of the carbohydrates with hydroxyl moieties results in a less well-ordered peptide conformation.Conclusions:It is likely that theN-acetyl groups of the carbohydrates have a critical role in promoting the more compact β-turn conformation through steric interactions with the peptide. This study has demonstrated that relatively small changes in carbohydrate composition can have dramatic ramifications on glycopeptide conformation.