Olson N H, Kolatkar P R, Oliveira M A, Cheng R H, Greve J M, McClelland A, Baker T S, Rossmann M G
Department of Biological Sciences, Purdue University, West Lafayette, IN 47907-1392.
Proc Natl Acad Sci U S A. 1993 Jan 15;90(2):507-11. doi: 10.1073/pnas.90.2.507.
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-A 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.
冷冻电子显微镜已被用于确定一种病毒与它的糖蛋白细胞受体结合时的结构。与细胞间黏附分子1的两个氨基末端免疫球蛋白样结构域结合的人鼻病毒16显示，细胞间黏附分子1结合到病毒表面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腔内的预测。与人类鼻病毒16和细胞间黏附分子1同源的人类鼻病毒14和CD4的原子结构与观察到的密度显示出极好的对应关系，从而确定了病毒与受体的相互作用。
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