Abstract
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).
Original language | English (US) |
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Pages (from-to) | 227-233 |
Number of pages | 7 |
Journal | Proteins: Structure, Function, and Bioinformatics |
Volume | 7 |
Issue number | 3 |
DOIs | |
State | Published - 1990 |
Externally published | Yes |
Keywords
- ICAM‐1
- docking receptor to virus
- immunoglobulin superfamily
- rhinovirus receptor
- structure prediction
ASJC Scopus subject areas
- Structural Biology
- Biochemistry
- Molecular Biology