CD2

CD2 interacts through its amino-terminal domain with the extracellular domain of CD58 (also designated CD2 ligand) to mediate cell adhesion. CD2/CD58 binding can enhance antigen-specific T cell activation. CD2 is a transmembrane glycoprotein that is expressed on peripheral blood T lymphocytes, NK cells and thymocytes. CD58 is a heavily glycosylated protein with a broad tissue distribution in hematopoietic and other cells, including endothelium. Interaction between CD2 and its counter receptor LFA3 (CD58) on opposing cells optimizes immune system recognition, thereby facilitating communication between helper T lymphocytes and antigen-presenting cells, as well as between cytolytic effectors and target cells.

[T-cell surface antigen CD2; T-cell surface antigen CD2; T-cell surface antigen CD2; LFA-3 receptor; rosette receptor; erythrocyte receptor; lymphocyte-function antigen-2; T-cell surface antigen T11/Leu-5; CD2 antigen (p50), sheep red blood cell receptor; CD2 molecule; Erythrocyte receptor; LFA-2; LFA-3 receptor; Rosette receptor; T-cell surface antigen T11/Leu-5; CD_antigen: CD2]