Cocrystal structure of the messenger RNA 5' cap-binding protein (eIF4E) bound to 7-methyl-GDP
Cocrystal structure of the messenger RNA 5' cap-binding protein (eIF4E) bound to 7-methyl-GDP
复制标题
DOI：
10.1016/s0092-8674(00)80280-9
复制
发表时间：
1997-06-13
期刊：
影响因子：
64.5
通讯作者：
Burley, SK
中科院分区：
文献类型：
--
作者：
Marcotrigiano, J;Gingras, AC;Burley, SK
在2.2埃分辨率下测定了与7-甲基- gdp结合的真核翻译起始因子4E （elF4E）的x射线结构。elF4E在翻译的限速起始步骤中识别5' 7-甲基- g (5')ppp(5')N mRNA帽。这种蛋白质类似于一只杯状的手，由一个弯曲的8股反平行的β薄片组成，后面是三个长长的α螺旋。7-甲基- gdp结合在分子凹表面的一个狭窄的帽结合槽中，其中7-甲基鸟嘌呤的识别是通过两个保守色氨酸之间的碱基夹心介导的，加上它的n7 -甲基和第三个保守色氨酸之间形成三个氢键和范德华接触。分子的凸背表面显示出系统发育保守的疏水/酸性部分，可能与其他翻译起始因子和调节蛋白相互作用。
The X-ray structure of the eukaryotic translation initiation factor 4E (elF4E), bound to 7-methyl-GDP, has been determined at 2.2 Angstrom resolution. elF4E recognizes 5' 7-methyl-G(5')ppp(5')N mRNA caps during the rate-limiting initiation step of translation. The protein resembles a cupped hand and consists of a curved, 8-stranded antiparallel beta sheet, backed by three long alpha helices. 7-methyl-GDP binds in a narrow cap-binding slot on the molecule's concave surface, where 7-methyl-guanine recognition is mediated by base sandwiching between two conserved tryptophans, plus formation of three hydrogen bonds and a van der Waals contact between its N7-methyl group and a third conserved tryptophan. The convex dorsal surface of the molecule displays a phylogenetically conserved hydrophobic/acidic portion, which may interact with other translation initiation factors and regulatory proteins.