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CD2 molecule

The protein structure of CD2. From PDB 1hnf
Available structures
1cdb, 1gya, 1hnf, 1qa9
Identifiers
Symbols CD2; SRBC; T11
External IDs OMIM186990 MGI88320 HomoloGene1338 GeneCards: CD2 Gene
RNA expression pattern
PBB GE CD2 205831 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 914 12481
Ensembl ENSG00000116824 ENSMUSG00000027863
UniProt P06729 Q5SRC1
RefSeq (mRNA) NM_001767 NM_013486
RefSeq (protein) NP_001758 NP_038514
Location (UCSC) Chr 1:
117.1 - 117.11 Mb
Chr 3:
101.4 - 101.42 Mb
PubMed search [1] [2]

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.[1]

Contents

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.[2]

In addition to its adhesive properties, CD2 also acts as a co-stimulatory molecule on T and NK cells.[3]

Classification

Due to its structural characteristics, CD2 is a member of the immunoglobulin superfamily; it possesses two immunoglobulin-like domains in its extracellular portion.[3]

Interactions

CD2 has been shown to interact with CD2BP2,[4] Lck[5] and PSTPIP1.[6]

References

  1. ^ Uniprot database entry for CD2 (accession number P06729)
  2. ^ 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. doi:10.2174/1389203033487063. PMID 14529530.  
  3. ^ 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. doi:10.2174/1389203013381251. PMID 12369898.  
  4. ^ Nishizawa, K; Freund C, Li J, Wagner G, Reinherz E L (Dec. 1998). "Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 95 (25): 14897–902. ISSN 0027-8424. PMID 9843987.  
  5. ^ Bell, G M; Fargnoli J, Bolen J B, Kish L, Imboden J B (Jan. 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. ISSN 0022-1007. PMID 8551220.  
  6. ^ Li, J; Nishizawa K, An W, Hussey R E, Lialios F E, Salgia R, Sunder-Plassmann R, Reinherz E L (Dec. 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. doi:10.1093/emboj/17.24.7320. ISSN 0261-4189. PMID 9857189.  

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. PMID 2471997.  
  • Rouleau M, Mollereau B, Bernard A, et al. (1997). "CD2 induced apoptosis of peripheral T cells.". Transplant. Proc. 29 (5): 2377–8. doi:10.1016/S0041-1345(97)00410-7. PMID 9270771.  
  • Lüscher B (2001). "Function and regulation of the transcription factors of the Myc/Max/Mad network.". Gene 277 (1-2): 1–14. doi:10.1016/S0378-1119(01)00697-7. PMID 11602341.  
  • 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. doi:10.2174/1389203013381251. PMID 12369898.  
  • 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. doi:10.1084/jem.175.2.527. PMID 1346273.  
  • 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. PMID 1351089.  
  • 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. doi:10.1126/science.1377404. PMID 1377404.  
  • 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. doi:10.1016/0165-2478(92)90078-3. PMID 1385321.  
  • 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. doi:10.1016/0008-8749(91)90051-C. PMID 1832084.  
  • Schraven B, Samstag Y, Altevogt P, Meuer SC (1990). "Association of CD2 and CD45 on human T lymphocytes.". Nature 345 (6270): 71–4. doi:10.1038/345071a0. PMID 1970422.  
  • 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. PMID 1976695.  
  • 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. PMID 2111780.  
  • 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. doi:10.1073/pnas.84.10.3365. PMID 2437578.  
  • Peterson A, Seed B (1987). "Monoclonal antibody and ligand binding sites of the T cell erythrocyte receptor (CD2).". Nature 329 (6142): 842–6. doi:10.1038/329842a0. PMID 2444890.  
  • 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. doi:10.1073/pnas.84.9.2941. PMID 2883656.  
  • 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. doi:10.1073/pnas.85.5.1615. PMID 2894031.  
  • 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. PMID 2901953.  
  • 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. doi:10.1111/j.1365-3083.1986.tb01985.x. PMID 3085210.  
  • 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. doi:10.1073/pnas.83.22.8718. PMID 3490670.  

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