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Journal of Experimental Medicine, Vol 177, 1187-1192, Copyright © 1993 by Rockefeller University Press
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AR de Fougerolles, LB Klickstein and TA Springer
Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115.
Based on protein sequence, we have isolated a cDNA for intercellular adhesion molecule 3 (ICAM-3), the most recently defined counter- receptor for lymphocyte function-associated antigen 1 (LFA-1). Expression of the cDNA yields a product that reacts with monoclonal antibody to ICAM-3 and functions as a ligand for LFA-1. The deduced 518- amino acid sequence of the predicted mature protein defines a highly glycosylated type I integral membrane protein with five immunoglobulin (Ig)-like domains. The five Ig-like domains of ICAM-3 are highly homologous with those of human ICAM-1 (52% identity) and human ICAM-2 (37% identity).
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