| Title | Modeling of the human intercellular adhesion molecule-1, the human rhinovirus major group receptor. | ||
| Author | Giranda, V L; Chapman, M S; Rossmann, M G | ||
| Journal | Proteins | Publication Year/Month | 1990 |
| PMID | 1972986 | PMCID | -N/A- |
| Affiliation | 1.Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907. | ||
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 receptor attachment site, the canyon, on the human rhinovirus-14 (HRV14) surface in a manner consistent with most of the mutational data for ICAM-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).