CD2

CD2

CD2 molecule

The protein structure of CD2. From PDB 1hnf
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols  ; LFA-2; SRBC; T11
External IDs ChEMBL: GeneCards:
RNA expression pattern
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

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,[1] LFA-3 receptor, erythrocyte receptor and rosette receptor.[2]


Contents

  • Function 1
    • Diagnostic relevance 1.1
  • Classification 2
  • Interactions 3
  • References 4
  • Further reading 5
  • External links 6

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.[3]

In addition to its adhesive properties, CD2 also acts as a co-stimulatory molecule on T and NK cells.[4]

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.[5]

Classification

Due to its structural characteristics, CD2 is a member of the immunoglobulin superfamily; it possesses two immunoglobulin-like domains in its extracellular portion.[4]

Interactions

CD2 has been shown to interact with CD2BP2,[6] Lck[7] and PSTPIP1.[8]

References

  1. ^ Sanchez-Madrid F, Krensky AM, Ware CF, Robbins E, Strominger JL, Burakoff SJ,  
  2. ^ Uniprot database entry for CD2 (accession number P06729)
  3. ^ Wilkins A, Yang W, Yang J (2003). "Structural biology of the cell adhesion protein CD2: from molecular recognition to protein folding and design". Curr Protein Pept Sci 4 (5): 367–73.  
  4. ^ a b Yang J, Ye Y, Carroll A, Yang W, Lee H (2001). "Structural biology of the cell adhesion protein CD2: alternatively folded states and structure-function relation". Curr Protein Pept Sci 2 (1): 1–17.  
  5. ^ Leong, Anthony S-Y; Cooper, Kumarason; Leong, F Joel W-M (2003). Manual of Diagnostic Cytology (2 ed.). Greenwich Medical Media, Ltd. p. 61.  
  6. ^ Nishizawa, K; Freund C; Li J; Wagner G; Reinherz E L (December 1998). "Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation".  
  7. ^ Bell, G M; Fargnoli J; Bolen J B; Kish L; Imboden J B (January 1996). "The SH3 domain of p56lck binds to proline-rich sequences in the cytoplasmic domain of CD2". J. Exp. Med. (UNITED STATES) 183 (1): 169–78.  
  8. ^ Li, J; Nishizawa K; An W; Hussey R E; Lialios F E; Salgia R; Sunder-Plassmann R; Reinherz E L (December 1998). "A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion". EMBO J. (ENGLAND) 17 (24): 7320–36.  

Further reading

  • Sayre PH, Reinherz EL (1989). "Structure and function of the erythrocyte receptor CD2 on human T lymphocytes: a review.". Scand. J. Rheumatol. Suppl. 76: 131–44.  
  • Rouleau M, Mollereau B, Bernard A, et al. (1997). "CD2 induced apoptosis of peripheral T cells.". Transplant. Proc. 29 (5): 2377–8.  
  • Lüscher B (2001). "Function and regulation of the transcription factors of the Myc/Max/Mad network.". Gene 277 (1-2): 1–14.  
  • Yang JJ, Ye Y, Carroll A, et al. (2002). "Structural biology of the cell adhesion protein CD2: alternatively folded states and structure-function relation.". Curr. Protein Pept. Sci. 2 (1): 1–17.  
  • Bell GM, Seaman WE, Niemi EC, Imboden JB (1992). "The OX-44 molecule couples to signaling pathways and is associated with CD2 on rat T lymphocytes and a natural killer cell line.". J. Exp. Med. 175 (2): 527–36.  
  • Marie-Cardine A, Maridonneau-Parini I, Ferrer M, et al. (1992). "The lymphocyte-specific tyrosine protein kinase p56lck is endocytosed in Jurkat cells stimulated via CD2.". J. Immunol. 148 (12): 3879–84.  
  • Hahn WC, Menu E, Bothwell AL, et al. (1992). "Overlapping but nonidentical binding sites on CD2 for CD58 and a second ligand CD59.". Science 256 (5065): 1805–7.  
  • Luzzati AL, Giacomini E, Giordani L, et al. (1992). "The antigen-specific induction of normal human lymphocytes in vitro is down-regulated by a conserved HIV p24 epitope.". Immunol. Lett. 33 (3): 307–14.  
  • Ruegg CL, Strand M (1991). "A synthetic peptide with sequence identity to the transmembrane protein GP41 of HIV-1 inhibits distinct lymphocyte activation pathways dependent on protein kinase C and intracellular calcium influx.". Cell. Immunol. 137 (1): 1–13.  
  • Schraven B, Samstag Y, Altevogt P, Meuer SC (1990). "Association of CD2 and CD45 on human T lymphocytes.". Nature 345 (6270): 71–4.  
  • Samelson LE, Fletcher MC, Ledbetter JA, June CH (1990). "Activation of tyrosine phosphorylation in human T cells via the CD2 pathway. Regulation by the CD45 tyrosine phosphatase.". J. Immunol. 145 (8): 2448–54.  
  • Luzzati AL, Pugliese O, Giacomini E, et al. (1990). "Immunoregulatory effect of a synthetic peptide corresponding to a region of protein p24 of HIV.". Folia Biol. (Praha) 36 (1): 71–7.  
  • Seed B, Aruffo A (1987). "Molecular cloning of the CD2 antigen, the T-cell erythrocyte receptor, by a rapid immunoselection procedure.". Proc. Natl. Acad. Sci. U.S.A. 84 (10): 3365–9.  
  • Peterson A, Seed B (1987). "Monoclonal antibody and ligand binding sites of the T cell erythrocyte receptor (CD2).". Nature 329 (6142): 842–6.  
  • Sayre PH, Chang HC, Hussey RE, et al. (1987). "Molecular cloning and expression of T11 cDNAs reveal a receptor-like structure on human T lymphocytes.". Proc. Natl. Acad. Sci. U.S.A. 84 (9): 2941–5.  
  • Diamond DJ, Clayton LK, Sayre PH, Reinherz EL (1988). "Exon-intron organization and sequence comparison of human and murine T11 (CD2) genes.". Proc. Natl. Acad. Sci. U.S.A. 85 (5): 1615–9.  
  • Lang G, Wotton D, Owen MJ, et al. (1988). "The structure of the human CD2 gene and its expression in transgenic mice.". EMBO J. 7 (6): 1675–82.  
  • Leca G, Boumsell L, Fabbi M, et al. (1986). "The sheep erythrocyte receptor and both alpha and beta chains of the human T-lymphocyte antigen receptor bind the mitogenic lectin (phytohaemagglutinin) from Phaseolus vulgaris.". Scand. J. Immunol. 23 (5): 535–44.  
  • Sewell WA, Brown MH, Dunne J, et al. (1986). "Molecular cloning of the human T-lymphocyte surface CD2 (T11) antigen.". Proc. Natl. Acad. Sci. U.S.A. 83 (22): 8718–22.  

External links

  • CD2 Antigen at the US National Library of Medicine Medical Subject Headings (MeSH)
  • Mouse CD Antigen Chart
  • Human CD Antigen Chart