Modelling of the human intercellular adhesion molecule‐1, the human rhinovirus major group receptor
- 1 January 1990
- journal article
- research article
- Published by Wiley in Proteins-Structure Function and Bioinformatics
- Vol. 7 (3) , 227-233
- https://doi.org/10.1002/prot.340070304
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).Keywords
This publication has 35 references indexed in Scilit:
- Crystal structure of human rhinovirus serotype 1A (HRV1A)Journal of Molecular Biology, 1989
- The Immunoglobulin Superfamily—Domains for Cell Surface RecognitionAnnual Review of Immunology, 1988
- Common cold virusesTrends in Biochemical Sciences, 1987
- Cell surface receptors for picornavirusesBioEssays, 1986
- The T4 gene encodes the AIDS virus receptor and is expressed in the immune system and the brainCell, 1986
- Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 Å and 1.9 Å resolutionJournal of Molecular Biology, 1980
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977
- Exploring structural homology of proteinsJournal of Molecular Biology, 1976
- Computer manipulation of (macro)molecules with the method of local changeActa Crystallographica Section A, 1974
- Chemical and biological evolution of a nucleotide-binding proteinNature, 1974