STRUCTURE OF A HUMAN RHINOVIRUS COMPLEXED WITH ITS RECEPTOR MOLECULE
STRUCTURE OF A HUMAN RHINOVIRUS COMPLEXED WITH ITS RECEPTOR MOLECULE
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DOI：
10.1073/pnas.90.2.507
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发表时间：
1993-01-15
影响因子：
11.1
通讯作者：
ROSSMANN, MG
中科院分区：
文献类型：
--
作者：
OLSON, NH;KOLATKAR, PR;ROSSMANN, MG
冷冻电子显微镜已被用来确定病毒与其糖蛋白细胞受体复合时的结构。与细胞间粘附分子1的两个氨基末端免疫球蛋白样结构域复合的人鼻病毒16显示，细胞间粘附分子1结合到病毒表面上12埃深的“峡谷”中。这一结果证实了病毒受体附着位点位于宿主抗体无法进入的空腔中的预测。人鼻病毒14和CD4的原子结构与人鼻病毒16和细胞间粘附分子1同源，与观察到的密度表现出良好的对应性，从而建立了病毒-受体相互作用。
Cryoelectron microscopy has been used to determine the structure of a virus when complexed with its glycoprotein cellular receptor. Human rhinovirus 16 complexed with the two amino-terminal, immunoglobulin-like domains of the intercellular adhesion molecule 1 shows that the intercellular adhesion molecule 1 binds into the 12-angstrom deep ''canyon'' on the viral surface. This result confirms the prediction that the viral-receptor attachment site lies in a cavity inaccessible to the host's antibodies. The atomic structures of human rhinovirus 14 and CD4, homologous to human rhinovirus 16 and intercellular adhesion molecule 1, showed excellent correspondence with observed density, thus establishing the virus-receptor interactions.