Structure of the glycosylated adhesion domain of human T lymphocyte glycoprotein CD2.
Withka, J.M., Wyss, D.F., Wagner, G., Arulanandam, A.R., Reinherz, E.L., Recny, M.A.(1993) Structure 1: 69-81
- PubMed: 7915183 
- DOI: https://doi.org/10.1016/0969-2126(93)90009-6
- Primary Citation of Related Structures:  
1CDB - PubMed Abstract: 
CD2, a T-cell specific surface glycoprotein, is critically important for mediating adherence of T cells to antigen-presenting cells or target cells. Domain 1 of human CD2 is responsible for cell adhesion, binding to CD58 (LFA-3) expressed on the cell to which the T cell binds. Human CD2 domain 1 requires N-linked carbohydrate to maintain its native conformation and ability to bind CD58. In contrast, rat CD2 does not require N-linked carbohydrate, and binds to a different ligand, CD48.
Organizational Affiliation: 
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.