CD2

CD2 molecule
	; The protein structure of CD2. From PDB 1hnf
Available structures
PDB	1CDB, 1GYA, 1HNF, 1L2Z, 1QA9, 2J6O, 2J7I
Identifiers
Symbols	CD2; FLJ46032; SRBC; T11
External IDs	OMIM: 186990 MGI: 88320 HomoloGene: 1338 GeneCards: CD2 Gene
Gene Ontology
Molecular function	• receptor activity; • protein binding; • protein homodimerization activity; • eukaryotic cell surface binding;
Cellular component	• extracellular region; • plasma membrane; • integral to plasma membrane; • external side of plasma membrane; • internal side of plasma membrane; • anchored to plasma membrane;
Biological process	• membrane raft polarization; • induction of apoptosis; • cell surface receptor linked signaling pathway; • blood coagulation; • cell-cell adhesion; • natural killer cell activation; • positive regulation of myeloid dendritic cell activation; • T cell activation; • regulation of T cell differentiation; • leukocyte migration;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs

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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]

[edit] 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]

[edit] 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.^[4]

[edit] 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]

[edit] Interactions

CD2 has been shown to interact with CD2BP2,^[5] Lck^[6] and PSTPIP1.^[7]

[edit] References

^ Uniprot database entry for CD2 (accession number P06729)
^ 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.
^ ^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.
^ Leong, Anthony S-Y; Cooper, Kumarason; Leong, F Joel W-M (2003). Manual of Diagnostic Cytology (2 ed.). Greenwich Medical Media, Ltd.. p. 61. ISBN 1 84110 100 1.
^ 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. doi:10.1073/pnas.95.25.14897. ISSN 0027-8424. PMC 24547. PMID 9843987. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=24547.
^ 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. doi:10.1084/jem.183.1.169. ISSN 0022-1007. PMC 2192399. PMID 8551220. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2192399.
^ 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. PMC 1171078. PMID 9857189. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1171078.

[edit] 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. PMC 2119111. PMID 1346273. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2119111.
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. PMC 304871. PMID 2437578. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=304871.
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. PMC 304776. PMID 2883656. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=304776.
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. PMC 279824. PMID 2894031. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=279824.
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. PMC 457152. PMID 2901953. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=457152.
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. PMC 387002. PMID 3490670. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=387002.

[edit] External links

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[0] Uniprot database entry for CD2 (accession number P06729)

[1] 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.

[yang-2] 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.

[Leong-3] Leong, Anthony S-Y; Cooper, Kumarason; Leong, F Joel W-M (2003). Manual of Diagnostic Cytology (2 ed.). Greenwich Medical Media, Ltd.. p. 61. ISBN 1 84110 100 1.

[pmid9843987-4] 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. doi:10.1073/pnas.95.25.14897. ISSN 0027-8424. PMC 24547. PMID 9843987. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=24547.

[pmid8551220-5] 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. doi:10.1084/jem.183.1.169. ISSN 0022-1007. PMC 2192399. PMID 8551220. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2192399.

[pmid9857189-6] 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. PMC 1171078. PMID 9857189. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1171078.

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CD2

Contents

[edit] Function

[edit] Diagnostic relevance

[edit] Classification

[edit] Interactions

[edit] References

[edit] Further reading

[edit] External links

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