Land A, Braakman I
Department of Bio-Organic Chemistry, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.
Biochimie. 2001 Aug;83(8):783-90. doi: 10.1016/s0300-9084(01)01314-1.
The lumen of the endoplasmic reticulum (ER) provides a unique folding environment that is distinct from other organelles supporting protein folding. The relatively oxidizing milieu allows the formation of disulfide bonds. N-linked oligosaccharides that are attached during synthesis play multiple roles in the folding process of glycoproteins. They stabilize folded domains and increase protein solubility, which prevents aggregation of folding intermediates. Glycans mediate the interaction of newly synthesized glycoproteins with some resident ER folding factors, such as calnexin and calreticulin. Here we present an overview of the present knowledge on the folding process of the heavily glycosylated human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein in the ER.
内质网（ER）的内腔提供了一个独特的折叠环境，与其他支持蛋白质折叠的细胞器不同。相对氧化的环境允许形成二硫键。合成过程中连接的N-连接寡糖在糖蛋白的折叠过程中发挥多种作用。它们稳定折叠结构域并增加蛋白质溶解度，从而防止折叠中间体聚集。聚糖介导新合成的糖蛋白与一些内质网驻留折叠因子（如钙连蛋白和钙网蛋白）的相互作用。在这里，我们概述了目前关于重糖基化的1型人类免疫缺陷病毒（HIV-1）包膜糖蛋白在内质网中折叠过程的知识。
