Modelling of the human intercellular adhesion molecule‐1, the human rhinovirus major group receptor

Vincent L. Giranda, Michael S. Chapman, Michael G. Rossmann

Research output: Contribution to journalArticle

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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 languageEnglish (US)
Pages (from-to)227-233
Number of pages7
JournalProteins: Structure, Function, and Bioinformatics
Volume7
Issue number3
DOIs
StatePublished - 1990

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Keywords

  • ICAM‐1
  • docking receptor to virus
  • immunoglobulin superfamily
  • rhinovirus receptor
  • structure prediction

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

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