| Literature DB >> 7913361 |
M G Rossmann1, N H Olson, P R Kolatkar, M A Oliveira, R H Cheng, J M Greve, A McClelland, T S Baker.
Abstract
Cryoelectron microscopy has been used to determine the first structure of a virus when complexed with its glycoprotein cellular receptor. Human rhinovirus 16 (HRV16) complexed with the two amino-terminal, immunoglobulin-like domains of the intercellular adhesion molecule-1 (ICAM-1) shows that ICAM-1 binds into the 12 A deep "canyon" on the surface of the virus. This is consistent with the prediction that the viral receptor attachment site lies in a cavity inaccessible to the host's antibodies. The atomic structures of HRV14 and CD4, homologous to HRV16 and ICAM-1, showed excellent correspondence with observed density, thus establishing the virus-receptor interactions.Entities:
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Year: 1994 PMID: 7913361 PMCID: PMC4140090 DOI: 10.1007/978-3-7091-9326-6_51
Source DB: PubMed Journal: Arch Virol Suppl ISSN: 0939-1983