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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 (Glu37, Leu66, Ser68, and Gln75), that are predicted to lie on the CC'FG face of the Ig fold, play a dominant role in LFA-1 binding.

Original publication

DOI

10.1074/jbc.270.2.877

Type

Journal article

Journal

J biol chem

Publication Date

13/01/1995

Volume

270

Pages

877 - 884

Keywords

Amino Acid Sequence, Animals, Antigens, CD, Antigens, Differentiation, Base Sequence, Binding Sites, Cell Adhesion Molecules, Cell Line, DNA Primers, Humans, Lymphocyte Function-Associated Antigen-1, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Sequence Homology, Amino Acid