Modeling of the human intercellular adhesion molecule-1, the human rhinovirus major group receptor.
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).
Giranda
V L
VL
Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907.
Chapman
M S
MS
Rossmann
M G
MG
D000595:Amino Acid Sequence; D002448:Cell Adhesion; D015815:Cell Adhesion Molecules / Q000235:genetics; D003198:Computer Simulation; D006801:Humans; D007074:Immunoglobulin G / Q000235:genetics; D018799:Intercellular Adhesion Molecule-1; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D011487:Protein Conformation; D011991:Receptors, Virus / Q000235:genetics / Q000276:immunology; D012229:Rhinovirus / Q000235:genetics / Q000276:immunology
D015815:Cell Adhesion Molecules; D007074:Immunoglobulin G; D011991:Receptors, Virus; D018799:Intercellular Adhesion Molecule-1