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PMID: 8093643 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Structure of a human rhinovirus complexed with its receptor molecule.

Olson NH, Kolatkar PR, Oliveira MA, Cheng RH, Greve JM, McClelland A, Baker TS, Rossmann MG

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.

MeSH Terms
Antigens, CD/metabolism,ultrastructure CD4 Antigens/metabolism,ultrastructure Cell Adhesion Molecules/metabolism,ultrastructure Cryopreservation Humans Image Processing, Computer-Assisted Intercellular Adhesion Molecule-1 Microscopy, Electron Models, Molecular Receptors, Virus/metabolism,ultrastructure Rhinovirus/metabolism,ultrastructure
Chemicals
Antigens, CD CD4 Antigens Cell Adhesion Molecules Receptors, Virus Intercellular Adhesion Molecule-1
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Olson N H
Department of Biological Sciences, Purdue University, West Lafayette, IN 47907-1392.
Kolatkar P R
Oliveira M A
Cheng R H
Greve J M
McClelland A
Baker T S
Rossmann M G
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1993-01-15
Pages
507-11
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC45692
Subset
IM
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