Botos Istvan, Wlodawer Alexander
Macromolecular Crystallography Laboratory, National Cancer Institute, NCI-Frederick, Building 536, Room 5, Frederick, MD 21702-1201, USA.
Prog Biophys Mol Biol. 2005 Jun;88(2):233-82. doi: 10.1016/j.pbiomolbio.2004.05.001.
A broad range of proteins bind high-mannose carbohydrates found on the surface of the envelope protein gp120 of the human immunodeficiency virus and thus interfere with the viral life cycle, providing a potential new way of controlling HIV infection. These proteins interact with the carbohydrate moieties in different ways. A group of them interacts as typical C-type lectins via a Ca2+ ion. Another group interacts with specific single, terminal sugars, without the help of a metal cation. A third group is involved in more intimate interactions, with multiple carbohydrate rings and no metal ion. Finally, there is a group of lectins for which the interaction mode has not yet been elucidated. This review summarizes, principally from a structural point of view, the current state of knowledge about these high-mannose binding proteins and their mode of sugar binding.
多种蛋白质可结合人类免疫缺陷病毒包膜蛋白gp120表面的高甘露糖碳水化合物,从而干扰病毒生命周期,为控制HIV感染提供了一种潜在的新方法。这些蛋白质以不同方式与碳水化合物部分相互作用。其中一组通过Ca2+离子作为典型的C型凝集素相互作用。另一组在没有金属阳离子帮助的情况下与特定的单个末端糖相互作用。第三组参与更紧密的相互作用,与多个碳水化合物环且无金属离子。最后,有一组凝集素,其相互作用模式尚未阐明。本综述主要从结构角度总结了关于这些高甘露糖结合蛋白及其糖结合模式的当前知识状态。