Shental-Bechor Dalit, Levy Yaakov
Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel.
Curr Opin Struct Biol. 2009 Oct;19(5):524-33. doi: 10.1016/j.sbi.2009.07.002. Epub 2009 Aug 3.
Glycosylation is among the most common post-translational modifications that proteins undergo that may affect many of their activities. It may also modify the underlying energy landscape of glycoproteins in a way that their altered biophysical characteristics are linked to their bioactivity. Yet, the capability of glycosylation to modify thermodynamic and kinetic properties varies greatly between glycoproteins. Deciphering the 'glycosylation code' that dictates the interplay between the nature of the carbohydrates or the proteins and the biophysical properties of the glycosylated proteins is essential. In this article, we discuss how the size, number, and structure of glycans, as well as the attachment sites, may modulate the folding of glycoproteins. Understanding the cross-talks between the protein and the attached glycans at the molecular level may assist in tailoring the biophysical properties of proteins in general.
糖基化是蛋白质最常见的翻译后修饰之一，这种修饰可能会影响蛋白质的许多活性。它还可能以一种改变糖蛋白潜在能量格局的方式进行修饰，使其改变的生物物理特性与其生物活性相关联。然而，糖基化修饰热力学和动力学性质的能力在糖蛋白之间差异很大。破解决定碳水化合物或蛋白质性质与糖基化蛋白质生物物理性质之间相互作用的“糖基化密码”至关重要。在本文中，我们讨论了聚糖的大小、数量和结构以及连接位点如何调节糖蛋白的折叠。从分子水平理解蛋白质与连接的聚糖之间的相互作用，总体上可能有助于定制蛋白质的生物物理性质。
