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Modelling of the human intercellular adhesion molecule‐1, the human rhinovirus major group receptor
Author(s) -
Giranda Vincent L.,
Chapman Michael S.,
Rossmann Michael G.
Publication year - 1990
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340070304
Subject(s) - rhinovirus , intercellular adhesion molecule 1 , intercellular adhesion molecule , receptor , intracellular , adhesion , cell adhesion molecule , group (periodic table) , chemistry , microbiology and biotechnology , cell adhesion , immunology , biology , biochemistry , virus , organic chemistry
A model has been built of the amino‐terminal domain of the intercellular adhesion molecule‐1 (ICAM‐1), the receptor for most human rhinovirus serotypes. The model was based on sequence and presumed structural homology to immunoglobulin constant domains. It fits well into the putative receptors attachment site, the canyon, on the human rhinovirus‐14 (HRV14) surface in a manner consistent with most of the mutational data for ICMA‐1 (Staunton, D. E., Dustin, M. L., Erickson, H. P., Springer, T. A. Cell, in press, 1989) and HRV14 (Colonno, R. J., Condra, J. H., Mizutani, S., Callahan, P. L., Davies, M. E., Murcko, M. A. Proc. Natl. Acad. Sci. U.S.A. 85: 5449‐5453, 1988).