Abstract
Human lymphocytes bear an array of surface glycoprotein receptors that interact with ligands on the surface of other immune cells, such as antigen presenting cells, and are involved in processes of T-cell activation. One important player in this team is human CD2 which binds to the counter receptor CD58 (LFA3) of antigen-presenting cells. Human CD2 is a 50–55 kDa surface glycoprotein which is found on virtually all T lymphocytes as well as on natural killer cells. It initiates the adhesion of T lymphocytes to infected target cells and antigen presenting cells (APCs). At the N-terminus, it consists of two extracellular domains followed by a single transmembrane domain and a proline-rich cytoplasmatic tail of 117 residues which is required for CD2-mediated signal transduction. All adhesion function of CD2 is mediated via the N-terminal adhesion domain. CD2 was predicted to be a member of the immunoglobulin superfamily (IgSF)1 based on sequence homology of its N-terminal domain and its membrane proximal second extracellular domain to variable and constant IgSF domains, respectively. Indeed, NMR solution studies of the adhesion domains of rat CD22 and human CD23 revealed conformations typical of immunoglobulin variable (V-set) domains. Furthermore, X-ray structures of the whole extracellular portions of rat CD24 and human CD25 confirmed this observation and also showed that the structures of the second extracellular domains are similar to constant (C2-set) domains of immunoglobulins. The two extracellular domains form a head-to-tail assembly in which the long axes of the two domains form an angle of ca 40°. However, the relative orientation of the two domains differs by ca. 20° between the rat and the human protein5 indicating that the two domains may have a certain mobility relative to each other in solution.
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Wagner, G. et al. (1996). Conformation, Mobility, and Function of the N-Linked Glycan in the Adhesion Domain of Human CD2. In: Jardetzky, O., Lefèvre, JF. (eds) Dynamics and the Problem of Recognition in Biological Macromolecules. NATO ASI Series, vol 288. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5839-2_18
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DOI: https://doi.org/10.1007/978-1-4615-5839-2_18
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