The domain structure of ICAM-1 and the kinetics of binding to rhinovirus
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Updated: Aug 8, 2026

A Liquid Phase Affinity Capture Assay Using Magnetic Beads to Study Protein-Protein Interaction: The Poliovirus-Nanobody Example
Published on: May 29, 2012
J M Casasnovas1, J K Bickford, T A Springer
1The Center for Blood Research and Harvard Medical School Department of Pathology, Boston, Massachusetts 02115, USA.
Abstract:
Fragments of intercellular adhesion molecule 1 (ICAM- 1) containing only the two most N terminal of its five immunoglobulin SF domains bind to rhinovirus 3 with the same affinity and kinetics as a fragment with the entire extracellular domain. The fully active two-domain fragments contain 5 or 14 more residues than a previously described fragment that is only partially active. Comparison of X-ray crystal structures show differences at the bottom of domain 2. Four different glycoforms of ICAM- 1 bind with identical kinetics.
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