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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1993 Jan 15;90(2):507–511. doi: 10.1073/pnas.90.2.507

Structure of a human rhinovirus complexed with its receptor molecule.

N H Olson 1, P R Kolatkar 1, M A Oliveira 1, R H Cheng 1, J M Greve 1, A McClelland 1, T S Baker 1, M G Rossmann 1
PMCID: PMC45692  PMID: 8093643

Abstract

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.

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Selected References

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