CD2

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1CDB, 1GYA, 1HNF, 1L2Z, 1QA9, 2J6O, 2J7I

Identifiers

Aliases

CD2, LFA-2, SRBC, T11, CD2 molecule

External IDs

OMIM: 186990 MGI: 88320 HomoloGene: 1338 GeneCards: CD2

Gene ontology
Molecular function	• protein homodimerization activity • protein binding • receptor binding • receptor activity
Cellular component	• integral component of membrane • membrane • cell-cell junction • anchored component of plasma membrane • plasma membrane • integral component of plasma membrane • extracellular region • cell surface • cytoplasmic side of plasma membrane • external side of plasma membrane
Biological process	• single organismal cell-cell adhesion • positive regulation of myeloid dendritic cell activation • heterotypic cell-cell adhesion • natural killer cell activation • membrane raft polarization • cell surface receptor signaling pathway • cell adhesion • positive regulation of interferon-gamma secretion • positive regulation of tumor necrosis factor production • positive regulation of interleukin-8 secretion • T cell activation • leukocyte migration • regulation of T cell differentiation • apoptotic process
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


914


12481

Ensembl


ENSG00000116824


ENSMUSG00000027863

UniProt


P06729 Q53F96


P08920

RefSeq (mRNA)


NM_001767 NM_001328609


NM_013486

RefSeq (protein)


NP_001758.2 NP_001758.2


NP_038514.1

Location (UCSC)

Chr 1: 116.75 – 116.77 Mb

Chr 3: 101.28 – 101.29 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

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,^[3] LFA-3 receptor, erythrocyte receptor and rosette receptor.^[4]

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.^[5]

In addition to its adhesive properties, CD2 also acts as a co-stimulatory molecule on T and NK cells.^[6]

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.^[7]

Classification

Due to its structural characteristics, CD2 is a member of the immunoglobulin superfamily; it possesses two immunoglobulin-like domains in its extracellular portion.^[6]

Interactions

CD2 has been shown to interact with CD2BP2,^[8] Lck^[9] and PSTPIP1.^[10]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Sanchez-Madrid F, Krensky AM, Ware CF, Robbins E, Strominger JL, Burakoff SJ, Springer TA (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. 79 (23): 7489–93. doi:10.1073/pnas.79.23.7489. PMC 347365. PMID 6984191.
↑ Uniprot database entry for CD2 (accession number P06729)
↑ Wilkins AL, Yang W, Yang JJ (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.
1 2 Yang JJ, Ye Y, Carroll A, Yang W, Lee HW (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 EL (December 1998). "Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation". Proc. Natl. Acad. Sci. U.S.A. 95 (25): 14897–902. doi:10.1073/pnas.95.25.14897. PMC 24547. PMID 9843987.
↑ Bell GM, Fargnoli J, Bolen JB, Kish L, Imboden JB (January 1996). "The SH3 domain of p56lck binds to proline-rich sequences in the cytoplasmic domain of CD2". J. Exp. Med. 183 (1): 169–78. doi:10.1084/jem.183.1.169. PMC 2192399. PMID 8551220.
↑ Li J, Nishizawa K, An W, Hussey RE, Lialios FE, Salgia R, Sunder-Plassmann R, Reinherz EL (December 1998). "A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion". EMBO J. 17 (24): 7320–36. doi:10.1093/emboj/17.24.7320. PMC 1171078. PMID 9857189.

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, Metivier D, Rosenthal-Allieri MA, Charpentier B, Senik A (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, Yang W, Lee HW (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.
Marie-Cardine A, Maridonneau-Parini I, Ferrer M, Danielian S, Rothhut B, Fagard R, Dautry-Varsat A, Fischer S (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, Sims PJ, Bierer BE (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, Pugliese O, Viora M, Chersi A (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, Giordani L, Quintieri F, Hraba T, Mach O, Krchnák V, Vágner J (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.
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, Brown NR, Richardson NE, Spagnoli G, Clayton LK, Reinherz EL (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.
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.
Lang G, Wotton D, Owen MJ, Sewell WA, Brown MH, Mason DY, Crumpton MJ, Kioussis D (1988). "The structure of the human CD2 gene and its expression in transgenic mice.". EMBO J. 7 (6): 1675–82. PMC 457152. PMID 2901953.
Leca G, Boumsell L, Fabbi M, Reinherz EL, Kanellopoulos JM (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, Owen MJ, Crumpton MJ (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.

PDB gallery

1cdb: STRUCTURE OF THE GLYCOSYLATED ADHESION DOMAIN OF HUMAN T LYMPHOCYTE GLYCOPROTEIN CD2

1gya: N-GLYCAN AND POLYPEPTIDE NMR SOLUTION STRUCTURES OF THE ADHESION DOMAIN OF HUMAN CD2

1hnf: CRYSTAL STRUCTURE OF THE EXTRACELLULAR REGION OF THE HUMAN CELL ADHESION MOLECULE CD2 AT 2.5 ANGSTROMS RESOLUTION

1qa9: Structure of a Heterophilic Adhesion Complex Between the Human CD2 and CD58(LFA-3) Counter-Receptors

External links

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

Proteins: clusters of differentiation (see also list of human clusters of differentiation)

1-50	CD1 a-c 1A 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d CD13 CD14 CD15 CD16 A B CD18 CD19 CD20 CD21 CD22 CD23 CD24 CD25 CD26 CD27 CD28 CD29 CD30 CD31 CD32 A B CD33 CD34 CD35 CD36 CD37 CD38 CD39 CD40 CD41 CD42 a b c d CD43 CD44 CD45 CD46 CD47 CD48 CD49 a b c d e f CD50

51-100	CD51 CD52 CD53 CD54 CD55 CD56 CD57 CD58 CD59 CD61 CD62 E L P CD63 CD64 A B C CD66 a b c d e f CD68 CD69 CD70 CD71 CD72 CD73 CD74 CD78 CD79 a b CD80 CD81 CD82 CD83 CD84 CD85 a d e h j k CD86 CD87 CD88 CD89 CD90 CD91 - CD92 CD93 CD94 CD95 CD96 CD97 CD98 CD99 CD100

101-150	CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150

151-200	CD151 CD152 CD153 CD154 CD155 CD156 a b c CD157 CD158 (a d e i k) CD159 a c CD160 CD161 CD162 CD163 CD164 CD166 CD167 a b CD168 CD169 CD170 CD171 CD172 a b g CD174 CD177 CD178 CD179 a b CD180 CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200

201-250	CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 - CD248 CD249

251-300	CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD263 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299

301-350	CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350

Cluster of differentiation by lineage

Lymphoid

B cell

plasma cell: CD38
CD138

T/NK

T cell	Pan-T antigens: CD3 CD7 CD1 CD4 CD8 CD13 CD18 CD26 CD27 CD28

NK cell	CD16 CD56/NCAM CD57

All	CD2

All

Myeloid

CFU-GM/
Myelomonocyte

MEP

CFU-Meg	CD34/CD36 CD42 CD41/CD61

CFU-E	CD36 CD71

All (pan-myeloid)

CD13
CD33

Stem cell

CD34

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CD2