Pestova Tatyana V, Hellen Christopher U T
Department of Microbiology and Immunology, State University of New York Downstate Medical Center, Brooklyn, NY 11203, USA.
Cell. 2003 Dec 12;115(6):650-2. doi: 10.1016/s0092-8674(03)00981-4.
The structure of the eukaryotic initiation factor eIF4E bound to a cognate domain of eIF4G and m(7)GDP in this issue of Cell shows that these factors undergo coupled folding to form a stable complex with high cap binding activity that promotes efficient ribosomal attachment to mRNA during translation initiation.
本期《细胞》杂志中,真核生物起始因子eIF4E与eIF4G的同源结构域及m(7)GDP结合的结构表明,这些因子会进行偶联折叠,形成一个具有高帽结合活性的稳定复合物,在翻译起始过程中促进核糖体有效附着于mRNA。