Interplay between rolling and firm adhesion elucidated with a cell-free system engineered with two distinct receptor-ligand pairs.Eniola AO et al. . The interaction between integrin lymphocyte function-associated antigen-1 (LFA-1) and its ligand intercellular adhesion molecule-1 (ICAM-1) is critical in immunological and inflammatory reactions,The extracellular domains of LFA-1 are composed of the large and complex αL and β2 subunits (Song et al. 2005).

(Song et al. 2005) reported a 1.65-A-resolution crystal structure of the ICAM-3 N-terminal domain (D1) in complex with the ligand-binding domain of integrin alpha-L-beta-2.

The extracellular domain of LFA-1 are composed of the large and complex integrin α-L and β2 subunits. Pig ICAM-2 expressed on stable transfectants supported firm adhesion of cells expressing human LFA-1 (Godwin et al. 2004).

ICAM-5 (telencephalin) is expressed on telencephalic neurons. ICAM-5 may act as a major adhesion molecule for leukocyte binding to neurons by binding to integrin alpha-L-beta-2 (Tian et al. 2000).

ICAM-4 is a red cell intercellular adhesion molecule. Cell transfectants expressing various integrins were used to demonstrate that integrins alpha-L-beta-2, alpha-M-beta-2, and alpha-IIb-beta-3 bind specifically and dose dependently to the recombinant ICAM-4-Fc protein. Cell surface ICAM-4 interacts with the cell surface alpha-V-beta-3 integrin (Hermand et al. 2004).