Modeling of the human intercellular adhesion molecule-1, the human rhinovirus major group receptor

V. L. Giranda, Michael Chapman, M. G. Rossmann

Research output: Contribution to journalArticle

37 Citations (Scopus)

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 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).

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

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Rhinovirus
Intercellular Adhesion Molecule-1
Immunoglobulins

Keywords

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

ASJC Scopus subject areas

  • Genetics
  • Structural Biology
  • Biochemistry

Cite this

Modeling of the human intercellular adhesion molecule-1, the human rhinovirus major group receptor. / Giranda, V. L.; Chapman, Michael; Rossmann, M. G.

In: Proteins: Structure, Function and Genetics, Vol. 7, No. 3, 1990, p. 227-233.

Research output: Contribution to journalArticle

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