title: The domain structure of ICAM-1 and the kinetics of binding to rhinovirus.
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.
authors.affiliation: The Center for Blood Research and Harvard Medical School Department of Pathology, Boston, Massachusetts 02115, USA.
authors.forename: J M
authors.initials: JM
authors.lastname: Casasnovas
authors.forename: J K
authors.initials: JK
authors.lastname: Bickford
authors.forename: T A
authors.initials: TA
authors.lastname: Springer
mesh_terms: D000911:Antibodies, Monoclonal / Q000276:immunology; D006367:HeLa Cells; D006801:Humans; D018799:Intercellular Adhesion Molecule-1 / Q000737:chemistry* / Q000378:metabolism; D007700:Kinetics; D012229:Rhinovirus / Q000502:physiology*
chemical_list: D000911:Antibodies, Monoclonal; D018799:Intercellular Adhesion Molecule-1