CD2: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
m (Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}}))
 
(→‎External links: Adding link to CD2 gene details page and display in UCSC genome browser.)
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details.
{{Infobox_gene}}
-->{{PBB_Controls
'''CD2''' (cluster of differentiation 2) is a [[cell adhesion molecule]] found on the surface of [[T cell]]s and [[NK cell|natural killer (NK) cells]].   
| update_page = yes
It has also been called T-cell surface antigen T11/Leu-5, LFA-2,<ref>{{cite journal | vauthors = Sanchez-Madrid F, Krensky AM, Ware CF, Robbins E, Strominger JL, Burakoff SJ, Springer TA | title = Three distinct antigens associated with human T-lymphocyte-mediated cytolysis: LFA-1, LFA-2, and LFA-3 | journal = Proc Natl Acad Sci U S A | volume = 79 | issue = 23 | pages = 7489–93 | year = 1982 | pmid = 6984191 | pmc = 347365 | doi = 10.1073/pnas.79.23.7489 }}</ref> LFA-3 receptor, erythrocyte receptor and rosette receptor.<ref>[http://www.expasy.org/cgi-bin/niceprot.pl?P06729 Uniprot database entry for CD2 (accession number P06729)]</ref>
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = CD2 antigen.png
| image_source = The protein structure of CD2. From {{PDB|1hnf}}
| PDB = {{PDB2|1cdb}}, {{PDB2|1gya}}, {{PDB2|1hnf}}, {{PDB2|1qa9}}
| Name = CD2 molecule
  | HGNCid = 1639
| Symbol = CD2
| AltSymbols =; SRBC; T11
| OMIM = 186990
| ECnumber =
| Homologene = 1338
| MGIid = 88320
| GeneAtlas_image1 = PBB_GE_CD2_205831_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0001766 |text = lipid raft polarization}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0016337 |text = cell-cell adhesion}} {{GNF_GO|id=GO:0030101 |text = natural killer cell activation}} {{GNF_GO|id=GO:0030887 |text = positive regulation of myeloid dendritic cell activation}} {{GNF_GO|id=GO:0042110 |text = T cell activation}} {{GNF_GO|id=GO:0045580 |text = regulation of T cell differentiation}}
  | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 914
    | Hs_Ensembl = ENSG00000116824
    | Hs_RefseqProtein = NP_001758
    | Hs_RefseqmRNA = NM_001767
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 117098530
    | Hs_GenLoc_end = 117113373
    | Hs_Uniprot = P06729
    | Mm_EntrezGene = 12481
    | Mm_Ensembl = ENSMUSG00000027863
    | Mm_RefseqmRNA = NM_013486
    | Mm_RefseqProtein = NP_038514
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 101404969
    | Mm_GenLoc_end = 101417000
    | Mm_Uniprot = Q5SRC1
  }}
}}


'''CD2''' (cluster of differentiation 2) is a [[cell adhesion molecule]] found on the surface of [[T cell]]s and [[NK cell|natural killer (NK) cells]]. 
== Function ==
It has also been called T-cell surface antigen T11/Leu-5, LFA-2, LFA-3 receptor, erythrocyte receptor and rosette receptor.<ref>[http://www.expasy.org/cgi-bin/niceprot.pl?P06729| Uniprot database entry for CD2 (accession number P06729)]</ref>
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.<ref>{{cite journal | vauthors = Wilkins AL, Yang W, Yang JJ | title = Structural biology of the cell adhesion protein CD2: from molecular recognition to protein folding and design | journal = Curr Protein Pept Sci | volume = 4 | issue = 5 | pages = 367–73 | year = 2003 | pmid = 14529530 | doi = 10.2174/1389203033487063 }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
 
{{PBB_Summary
In addition to its adhesive properties, CD2 also acts as a [[co-stimulatory]] molecule on T and NK cells.<ref name = yang>{{cite journal | vauthors = Yang JJ, Ye Y, Carroll A, Yang W, Lee HW | title = Structural biology of the cell adhesion protein CD2: alternatively folded states and structure-function relation | journal = Curr Protein Pept Sci | volume = 2 | issue = 1 | pages = 1–17 | year = 2001 | pmid = 12369898 | doi = 10.2174/1389203013381251 }}</ref>
| section_title =
 
| summary_text =
=== Diagnostic relevance ===
}}
 
==Function==
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 [[lymphoma]]s and [[leukaemia]]s also express CD2, making it possible to use the presence of the antigen to distinguish these conditions from B cell [[neoplasm]]s.<ref name=Leong>{{cite book|author=Leong, Anthony S-Y|author2=Cooper, Kumarason|author3=Leong, F Joel W-M|year=2003|title=Manual of Diagnostic Cytology|edition=2|publisher=Greenwich Medical Media, Ltd.|page=61|isbn=1-84110-100-1}}</ref>
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.<ref>{{cite journal |author=Wilkins A, Yang W, Yang J |title=Structural biology of the cell adhesion protein CD2: from molecular recognition to protein folding and design |journal=Curr Protein Pept Sci |volume=4 |issue=5 |pages=367-73 |year=2003 |id=PMID 14529530}}</ref>


In addition to its adhesive properties, CD2 also acts as a [[co-stimulatory]] molecule on T and NK cells.<ref name = yang>{{cite journal |author=Yang J, Ye Y, Carroll A, Yang W, Lee H |title=Structural biology of the cell adhesion protein CD2: alternatively folded states and structure-function relation |journal=Curr Protein Pept Sci |volume=2 |issue=1 |pages=1-17 |year=2001 |id=PMID 12369898}}</ref>
== Classification ==


==Classification==
Due to its structural characteristics, CD2 is a member of the [[immunoglobulin superfamily]]; it possesses two immunoglobulin-like domains in its [[extracellular]] portion.<ref name = yang/>
Due to its structural characteristics, CD2 is a member of the [[immunoglobulin superfamily]]; it possesses two immunoglobulin-like domains in its [[extracellular]] portion.<ref name = yang/>


==References==
== Interactions ==
{{reflist|2}}
 
CD2 has been shown to [[Protein-protein interaction|interact]] with [[CD2BP2]],<ref name=pmid9843987>{{cite journal | vauthors = Nishizawa K, Freund C, Li J, Wagner G, Reinherz EL | title = Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation | journal = [[PNAS|Proc. Natl. Acad. Sci. U.S.A.]] | volume = 95 | issue = 25 | pages = 14897–902 | date = December 1998 | pmid = 9843987 | pmc = 24547 | doi = 10.1073/pnas.95.25.14897 }}</ref> [[Lck]]<ref name=pmid8551220>{{cite journal | vauthors = Bell GM, Fargnoli J, Bolen JB, Kish L, Imboden JB | title = The SH3 domain of p56lck binds to proline-rich sequences in the cytoplasmic domain of CD2 | journal = J. Exp. Med. | volume = 183 | issue = 1 | pages = 169–78 | date = January 1996 | pmid = 8551220 | pmc = 2192399 | doi = 10.1084/jem.183.1.169 }}</ref> and [[PSTPIP1]].<ref name=pmid9857189>{{cite journal | vauthors = Li J, Nishizawa K, An W, Hussey RE, Lialios FE, Salgia R, Sunder-Plassmann R, Reinherz EL | title = A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion | journal = EMBO J. | volume = 17 | issue = 24 | pages = 7320–36 | date = December 1998 | pmid = 9857189 | pmc = 1171078 | doi = 10.1093/emboj/17.24.7320 }}</ref>


==Further reading==
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Sayre PH, Reinherz EL | title = Structure and function of the erythrocyte receptor CD2 on human T lymphocytes: a review. | journal = Scand. J. Rheumatol. Suppl. | volume = 76 | issue =  | pages = 131–44 | year = 1989 | pmid = 2471997 | doi =  }}
| citations =
* {{cite journal | vauthors = Rouleau M, Mollereau B, Bernard A, Metivier D, Rosenthal-Allieri MA, Charpentier B, Senik A | title = CD2 induced apoptosis of peripheral T cells. | journal = Transplant. Proc. | volume = 29 | issue = 5 | pages = 2377–8 | year = 1997 | pmid = 9270771 | doi = 10.1016/S0041-1345(97)00410-7 }}
*{{cite journal | author=Sayre PH, Reinherz EL |title=Structure and function of the erythrocyte receptor CD2 on human T lymphocytes: a review. |journal=Scand. J. Rheumatol. Suppl. |volume=76 |issue=  |pages= 131-44 |year= 1989 |pmid= 2471997 |doi=  }}
* {{cite journal | vauthors = Lüscher B | title = Function and regulation of the transcription factors of the Myc/Max/Mad network. | journal = Gene | volume = 277 | issue = 1-2 | pages = 1–14 | year = 2001 | pmid = 11602341 | doi = 10.1016/S0378-1119(01)00697-7 }}
*{{cite journal | author=Rouleau M, Mollereau B, Bernard A, ''et al.'' |title=CD2 induced apoptosis of peripheral T cells. |journal=Transplant. Proc. |volume=29 |issue= 5 |pages= 2377-8 |year= 1997 |pmid= 9270771 |doi= }}
* {{cite journal | vauthors = Yang JJ, Ye Y, Carroll A, Yang W, Lee HW | title = Structural biology of the cell adhesion protein CD2: alternatively folded states and structure-function relation. | journal = Curr. Protein Pept. Sci. | volume = 2 | issue = 1 | pages = 1–17 | year = 2002 | pmid = 12369898 | doi = 10.2174/1389203013381251 }}
*{{cite journal | author=Lüscher B |title=Function and regulation of the transcription factors of the Myc/Max/Mad network. |journal=Gene |volume=277 |issue= 1-2 |pages= 1-14 |year= 2001 |pmid= 11602341 |doi= }}
* {{cite journal | vauthors = Bell GM, Seaman WE, Niemi EC, Imboden JB | title = The OX-44 molecule couples to signaling pathways and is associated with CD2 on rat T lymphocytes and a natural killer cell line. | journal = J. Exp. Med. | volume = 175 | issue = 2 | pages = 527–36 | year = 1992 | pmid = 1346273 | pmc = 2119111 | doi = 10.1084/jem.175.2.527 }}
*{{cite journal | author=Yang JJ, Ye Y, Carroll A, ''et al.'' |title=Structural biology of the cell adhesion protein CD2: alternatively folded states and structure-function relation. |journal=Curr. Protein Pept. Sci. |volume=2 |issue= 1 |pages= 1-17 |year= 2002 |pmid= 12369898 |doi= }}
* {{cite journal | vauthors = Marie-Cardine A, Maridonneau-Parini I, Ferrer M, Danielian S, Rothhut B, Fagard R, Dautry-Varsat A, Fischer S | title = The lymphocyte-specific tyrosine protein kinase p56lck is endocytosed in Jurkat cells stimulated via CD2. | journal = J. Immunol. | volume = 148 | issue = 12 | pages = 3879–84 | year = 1992 | pmid = 1351089 | doi =  }}
*{{cite journal | author=Bell GM, Seaman WE, Niemi EC, Imboden JB |title=The OX-44 molecule couples to signaling pathways and is associated with CD2 on rat T lymphocytes and a natural killer cell line. |journal=J. Exp. Med. |volume=175 |issue= 2 |pages= 527-36 |year= 1992 |pmid= 1346273 |doi= }}
* {{cite journal | vauthors = Hahn WC, Menu E, Bothwell AL, Sims PJ, Bierer BE | title = Overlapping but nonidentical binding sites on CD2 for CD58 and a second ligand CD59. | journal = Science | volume = 256 | issue = 5065 | pages = 1805–7 | year = 1992 | pmid = 1377404 | doi = 10.1126/science.1377404 }}
*{{cite journal | author=Marie-Cardine A, Maridonneau-Parini I, Ferrer M, ''et al.'' |title=The lymphocyte-specific tyrosine protein kinase p56lck is endocytosed in Jurkat cells stimulated via CD2. |journal=J. Immunol. |volume=148 |issue= 12 |pages= 3879-84 |year= 1992 |pmid= 1351089 |doi=  }}
* {{cite journal | vauthors = Luzzati AL, Giacomini E, Giordani L, Pugliese O, Viora M, Chersi A | title = The antigen-specific induction of normal human lymphocytes in vitro is down-regulated by a conserved HIV p24 epitope. | journal = Immunol. Lett. | volume = 33 | issue = 3 | pages = 307–14 | year = 1992 | pmid = 1385321 | doi = 10.1016/0165-2478(92)90078-3 }}
*{{cite journal | author=Hahn WC, Menu E, Bothwell AL, ''et al.'' |title=Overlapping but nonidentical binding sites on CD2 for CD58 and a second ligand CD59. |journal=Science |volume=256 |issue= 5065 |pages= 1805-7 |year= 1992 |pmid= 1377404 |doi= }}
* {{cite journal | vauthors = Ruegg CL, Strand M | title = 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. | journal = Cell. Immunol. | volume = 137 | issue = 1 | pages = 1–13 | year = 1991 | pmid = 1832084 | doi = 10.1016/0008-8749(91)90051-C }}
*{{cite journal | author=Luzzati AL, Giacomini E, Giordani L, ''et al.'' |title=The antigen-specific induction of normal human lymphocytes in vitro is down-regulated by a conserved HIV p24 epitope. |journal=Immunol. Lett. |volume=33 |issue= 3 |pages= 307-14 |year= 1992 |pmid= 1385321 |doi= }}
* {{cite journal | vauthors = Schraven B, Samstag Y, Altevogt P, Meuer SC | title = Association of CD2 and CD45 on human T lymphocytes. | journal = Nature | volume = 345 | issue = 6270 | pages = 71–4 | year = 1990 | pmid = 1970422 | doi = 10.1038/345071a0 }}
*{{cite journal | author=Ruegg CL, Strand M |title=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. |journal=Cell. Immunol. |volume=137 |issue= 1 |pages= 1-13 |year= 1991 |pmid= 1832084 |doi= }}
* {{cite journal | vauthors = Samelson LE, Fletcher MC, Ledbetter JA, June CH | title = Activation of tyrosine phosphorylation in human T cells via the CD2 pathway. Regulation by the CD45 tyrosine phosphatase. | journal = J. Immunol. | volume = 145 | issue = 8 | pages = 2448–54 | year = 1990 | pmid = 1976695 | doi =  }}
*{{cite journal | author=Schraven B, Samstag Y, Altevogt P, Meuer SC |title=Association of CD2 and CD45 on human T lymphocytes. |journal=Nature |volume=345 |issue= 6270 |pages= 71-4 |year= 1990 |pmid= 1970422 |doi= 10.1038/345071a0 }}
* {{cite journal | vauthors = Luzzati AL, Pugliese O, Giacomini E, Giordani L, Quintieri F, Hraba T, Mach O, Krchnák V, Vágner J | title = Immunoregulatory effect of a synthetic peptide corresponding to a region of protein p24 of HIV. | journal = Folia Biol. (Praha) | volume = 36 | issue = 1 | pages = 71–7 | year = 1990 | pmid = 2111780 | doi =  }}
*{{cite journal | author=Samelson LE, Fletcher MC, Ledbetter JA, June CH |title=Activation of tyrosine phosphorylation in human T cells via the CD2 pathway. Regulation by the CD45 tyrosine phosphatase. |journal=J. Immunol. |volume=145 |issue= 8 |pages= 2448-54 |year= 1990 |pmid= 1976695 |doi=  }}
* {{cite journal | vauthors = Seed B, Aruffo A | title = Molecular cloning of the CD2 antigen, the T-cell erythrocyte receptor, by a rapid immunoselection procedure. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 84 | issue = 10 | pages = 3365–9 | year = 1987 | pmid = 2437578 | pmc = 304871 | doi = 10.1073/pnas.84.10.3365 }}
*{{cite journal | author=Luzzati AL, Pugliese O, Giacomini E, ''et al.'' |title=Immunoregulatory effect of a synthetic peptide corresponding to a region of protein p24 of HIV. |journal=Folia Biol. (Praha) |volume=36 |issue= 1 |pages= 71-7 |year= 1990 |pmid= 2111780 |doi=  }}
* {{cite journal | vauthors = Peterson A, Seed B | title = Monoclonal antibody and ligand binding sites of the T cell erythrocyte receptor (CD2). | journal = Nature | volume = 329 | issue = 6142 | pages = 842–6 | year = 1987 | pmid = 2444890 | doi = 10.1038/329842a0 }}
*{{cite journal | author=Seed B, Aruffo A |title=Molecular cloning of the CD2 antigen, the T-cell erythrocyte receptor, by a rapid immunoselection procedure. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 10 |pages= 3365-9 |year= 1987 |pmid= 2437578 |doi= }}
* {{cite journal | vauthors = Sayre PH, Chang HC, Hussey RE, Brown NR, Richardson NE, Spagnoli G, Clayton LK, Reinherz EL | title = Molecular cloning and expression of T11 cDNAs reveal a receptor-like structure on human T lymphocytes. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 84 | issue = 9 | pages = 2941–5 | year = 1987 | pmid = 2883656 | pmc = 304776 | doi = 10.1073/pnas.84.9.2941 }}
*{{cite journal | author=Peterson A, Seed B |title=Monoclonal antibody and ligand binding sites of the T cell erythrocyte receptor (CD2). |journal=Nature |volume=329 |issue= 6142 |pages= 842-6 |year= 1987 |pmid= 2444890 |doi= 10.1038/329842a0 }}
* {{cite journal | vauthors = Diamond DJ, Clayton LK, Sayre PH, Reinherz EL | title = Exon-intron organization and sequence comparison of human and murine T11 (CD2) genes. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 85 | issue = 5 | pages = 1615–9 | year = 1988 | pmid = 2894031 | pmc = 279824 | doi = 10.1073/pnas.85.5.1615 }}
*{{cite journal | author=Sayre PH, Chang HC, Hussey RE, ''et al.'' |title=Molecular cloning and expression of T11 cDNAs reveal a receptor-like structure on human T lymphocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 9 |pages= 2941-5 |year= 1987 |pmid= 2883656 |doi= }}
* {{cite journal | vauthors = Lang G, Wotton D, Owen MJ, Sewell WA, Brown MH, Mason DY, Crumpton MJ, Kioussis D | title = The structure of the human CD2 gene and its expression in transgenic mice. | journal = EMBO J. | volume = 7 | issue = 6 | pages = 1675–82 | year = 1988 | pmid = 2901953 | pmc = 457152 | doi =  }}
*{{cite journal | author=Diamond DJ, Clayton LK, Sayre PH, Reinherz EL |title=Exon-intron organization and sequence comparison of human and murine T11 (CD2) genes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 5 |pages= 1615-9 |year= 1988 |pmid= 2894031 |doi= }}
* {{cite journal | vauthors = Leca G, Boumsell L, Fabbi M, Reinherz EL, Kanellopoulos JM | title = 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. | journal = Scand. J. Immunol. | volume = 23 | issue = 5 | pages = 535–44 | year = 1986 | pmid = 3085210 | doi = 10.1111/j.1365-3083.1986.tb01985.x }}
*{{cite journal | author=Lang G, Wotton D, Owen MJ, ''et al.'' |title=The structure of the human CD2 gene and its expression in transgenic mice. |journal=EMBO J. |volume=7 |issue= 6 |pages= 1675-82 |year= 1988 |pmid= 2901953 |doi=  }}
* {{cite journal | vauthors = Sewell WA, Brown MH, Dunne J, Owen MJ, Crumpton MJ | title = Molecular cloning of the human T-lymphocyte surface CD2 (T11) antigen. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 83 | issue = 22 | pages = 8718–22 | year = 1986 | pmid = 3490670 | pmc = 387002 | doi = 10.1073/pnas.83.22.8718 }}
*{{cite journal | author=Leca G, Boumsell L, Fabbi M, ''et al.'' |title=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. |journal=Scand. J. Immunol. |volume=23 |issue= 5 |pages= 535-44 |year= 1986 |pmid= 3085210 |doi= }}
*{{cite journal | author=Sewell WA, Brown MH, Dunne J, ''et al.'' |title=Molecular cloning of the human T-lymphocyte surface CD2 (T11) antigen. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 22 |pages= 8718-22 |year= 1986 |pmid= 3490670 |doi= }}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=914}}


==External links==
== External links ==
* {{MeshName|CD2+Antigen}}
* {{MeshName|CD2+Antigen}}
* [http://www.ebioscience.com/ebioscience/whatsnew/mousecdchart.htm Mouse CD Antigen Chart]
* [http://www.ebioscience.com/ebioscience/whatsnew/humancdchart.htm Human CD Antigen Chart]
* {{UCSC gene info|CD2}}


{{Clusters of differentiation}}
{{Clusters of differentiation}}
{{Clusters of differentiation by lineage}}


[[Category:clusters of differentiation]]
[[Category:Clusters of differentiation]]
 
 
{{protein-stub}}
 
[[ca:CD2]]
[[es:CD2]]
[[it:CD2]]
{{WikiDoc Sources}}

Revision as of 23:12, 15 March 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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]

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, 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.
  2. ↑ Uniprot database entry for CD2 (accession number P06729)
  3. ↑ 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.
  4. ↑ 4.0 4.1 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.
  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. ISBN 1-84110-100-1.
  6. ↑ 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.
  7. ↑ 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.
  8. ↑ 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.

Further reading

External links

Retrieved from "https://www.wikidoc.org/index.php?title=CD2&oldid=1410740"