Kostelansky Michael S, Sun Ji, Lee Sangho, Kim Jaewon, Ghirlando Rodolfo, Hierro Aitor, Emr Scott D, Hurley James H
Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US Department of Health and Human Services, Bethesda, MD 20892, USA.
Cell. 2006 Apr 7;125(1):113-26. doi: 10.1016/j.cell.2006.01.049.
The endosomal sorting complex required for transport (ESCRT) complexes are central to receptor downregulation, lysosome biogenesis, and budding of HIV. The yeast ESCRT-I complex contains the Vps23, Vps28, and Vps37 proteins, and its assembly is directed by the C-terminal steadiness box of Vps23, the N-terminal half of Vps28, and the C-terminal half of Vps37. The crystal structures of a Vps23:Vps28 core subcomplex and the Vps23:Vps28:Vps37 core were solved at 2.1 and 2.8 A resolution. Each subunit contains a structurally similar pair of helices that form the core. The N-terminal domain of Vps28 has a hydrophobic binding site on its surface that is conformationally dynamic. The C-terminal domain of Vps28 binds the ESCRT-II complex. The structure shows how ESCRT-I is assembled by a compact core from which the Vps23 UEV domain, the Vps28 C domain, and other domains project to bind their partners.
转运所需的内体分选复合物（ESCRT）对于受体下调、溶酶体生物发生和HIV出芽至关重要。酵母ESCRT-I复合物包含Vps23、Vps28和Vps37蛋白，其组装由Vps23的C端稳定盒、Vps28的N端一半以及Vps37的C端一半指导。Vps23:Vps28核心亚复合物和Vps23:Vps28:Vps37核心的晶体结构分别以2.1埃和2.8埃的分辨率解析。每个亚基都包含一对结构相似的螺旋，形成核心。Vps28的N端结构域在其表面有一个构象动态的疏水结合位点。Vps28的C端结构域结合ESCRT-II复合物。该结构展示了ESCRT-I是如何由一个紧凑的核心组装而成，Vps23 UEV结构域、Vps28 C结构域和其他结构域从该核心伸出以结合它们的伙伴。
