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Volume 270, Number 2, Issue of January 13, 1995 pp. 877-884
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Analysis of the Binding Site on Intercellular Adhesion Molecule 3 for the Leukocyte Integrin Lymphocyte Function-associated Antigen 1

(Received for publication, August 29, 1994; and in revised form, November 8, 1994)

Claire L. Holness ,  Paul A. Bates ,  Amanda J. Littler ,  Christopher D. Buckley ,  Alison McDowall ,  David Bossy ,  Nancy Hogg ,  David L. Simmons

Intercellular adhesion molecule 3 (ICAM-3, CD50) is a member of the immunoglobulin superfamily and is a constitutively expressed ligand for the leukocyte integrin LFA-1 (CD11a/CD18). ICAM-3 is expressed at high levels by all resting leukocyte populations and antigen presenting cells and is a major ligand for LFA-1 in the resting immune system. ICAM-3 is a signal transducer and may play a key role in initiating immune responses. Mutant ICAM-3 Fc-chimeric proteins were quantitatively analyzed for their ability to bind COS cells expressing human LFA-1. The LFA-1-binding site on ICAM-3 is located in the N-terminal 2 Ig domains. Domains 3-5 do not significantly contribute to adhesion. The binding site has been further resolved by rational targeting of 14 point mutations throughout domains 1 and 2, coupled with modeling studies. Within domain 1 a cluster of residues (Glu, Leu, Ser, and Gln), that are predicted to lie on the CC`FG face of the Ig fold, play a dominant role in LFA-1 binding.



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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.