Laboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, NIH, Bethesda, MD 20892, USA.
Curr Opin Struct Biol. 2013 Apr;23(2):268-76. doi: 10.1016/j.sbi.2013.03.007. Epub 2013 Apr 18.
The trimeric envelope glycoprotein of HIV-1, composed of gp120 and gp41 subunits, remains a major target for vaccine development. The structures of the core regions of monomeric gp120 and gp41 have been determined previously by X-ray crystallography. New insights into the structure of trimeric HIV-1 envelope glycoproteins are now coming from cryo-electron tomographic studies of the gp120/gp41 trimer as displayed on intact viruses and from cryo-electron microscopic studies of purified, soluble versions of the ectodomain of the trimer. Here, we review recent developments in these fields as they relate to our understanding of the structure and function of HIV-1 envelope glycoproteins.
HIV-1 的三聚体包膜糖蛋白由 gp120 和 gp41 亚基组成,仍然是疫苗开发的主要目标。先前已经通过 X 射线晶体学确定了单体 gp120 和 gp41 的核心区域的结构。现在,来自完整病毒上展示的 gp120/gp41 三聚体的低温电子断层扫描研究和三聚体外域的纯化可溶性形式的低温电子显微镜研究为了解 HIV-1 包膜糖蛋白的结构和功能提供了新的见解。在这里,我们回顾了这些领域的最新进展,因为它们与我们对 HIV-1 包膜糖蛋白的结构和功能的理解有关。