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CD2

Cell adhesion molecule found on the surface of T cells and natural killer


Summary

Cell adhesion molecule found on the surface of T cells and natural killer

CD2 (cluster of differentiation 2) is a cell adhesion molecule found on the surface of T cells and natural killer (NK) cells. It has also been called T-cell surface antigen T11/Leu-5, LFA-2, LFA-3 receptor, erythrocyte receptor and rosette receptor.

Function

It interacts with other adhesion molecules, such as lymphocyte function-associated antigen-3 (LFA-3/CD58) in humans, or CD48 in rodents, which are expressed on the surfaces of other cells.

In addition to its adhesive properties, CD2 also acts as a co-stimulatory molecule on T and NK cells.

Diagnostic relevance

CD2 is a specific marker for T cells and NK cells, and can therefore be used in immunohistochemistry to identify the presence of such cells in tissue sections. The great majority of T cell lymphomas and leukaemias also express CD2, making it possible to use the presence of the antigen to distinguish these conditions from B cell neoplasms.

Classification

Due to its structural characteristics, CD2 is a member of the immunoglobulin superfamily; it possesses two immunoglobulin-like domains in its extracellular portion.

Interactions

CD2 has been shown to interact with CD2BP2, Lck and PSTPIP1.

References

References

  1. (1982). "Three distinct antigens associated with human T-lymphocyte-mediated cytolysis: LFA-1, LFA-2, and LFA-3". Proc Natl Acad Sci U S A.
  2. [http://www.expasy.org/cgi-bin/niceprot.pl?P06729 Uniprot database entry for CD2 (accession number P06729)]
  3. (2003). "Structural biology of the cell adhesion protein CD2: from molecular recognition to protein folding and design". Curr Protein Pept Sci.
  4. (2001). "Structural biology of the cell adhesion protein CD2: alternatively folded states and structure-function relation". Curr Protein Pept Sci.
  5. Leong, Anthony S-Y. (2003). "Manual of Diagnostic Cytology". Greenwich Medical Media, Ltd..
  6. (December 1998). "Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation". [[PNAS.
  7. (January 1996). "The SH3 domain of p56lck binds to proline-rich sequences in the cytoplasmic domain of CD2". [[Journal of Experimental Medicine]].
  8. (December 1998). "A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion". EMBO J..
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