Structure and function of the erythrocyte receptor CD2 on human T lymphocytes: a review.

The human CD2 molecule is a 50kd surface glycoprotein expressed on greater than 95% of thymocytes and all peripheral T lymphocytes which mediates both adhesion between T cells and their targets, and subsequent T cell activation events. Molecular cloning of human CD2 cDNAs predicts a mature CD2 protein of 327 amino acids, with an extracellular segment of 185 amino acids, a transmembrane domain of 24 amino acids and an intracytoplasmic region of 117 amino acids. Genomic cloning shows that the extracellular segment is encoded by two exons, the transmembrane segment by a single exon and the intracytoplasmic region by a single exon. Expression and biochemical analysis of a soluble extracellular domain CD2 molecule reveal that it expresses native CD2 epitopes and contains a stable 15kd NH2-terminal fragment corresponding to a single exon. Binding analyses of the soluble CD2 molecule indicate that it binds specifically to a known cell-surface ligand for CD2 at a relatively low affinity, thus suggesting that T cell-target adhesion mediated by CD2 and its ligand depends on multimeric attachment between an array of CD2 molecules and their cognate ligands.

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