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CD2

From Wikipedia, the free encyclopedia

Cell adhesion molecule found on the surface of T cells and natural killer
CD2
Available structures
PDBOrtholog search:PDBeRCSB
List of PDB id codes

1CDB,1GYA,1HNF,1L2Z,1QA9,2J6O,2J7I

Identifiers
AliasesCD2, LFA-2, SRBC, T11, CD2 molecule
External IDsOMIM:186990;MGI:88320;HomoloGene:1338;GeneCards:CD2;OMA:CD2 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for CD2
Genomic location for CD2
Band1p13.1Start116,754,430bp[1]
End116,769,229bp[1]
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)[2]
Chromosome 3 (mouse)
Genomic location for CD2
Genomic location for CD2
Band3 F2.2|3 44.17 cMStart101,183,215bp[2]
End101,195,255bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • granulocyte

  • thymus

  • lymph node

  • testicle

  • appendix

  • blood

  • epithelium of nasopharynx

  • superficial temporal artery

  • spleen

  • mucosa of ileum
Top expressed in
  • thymus

  • mesenteric lymph nodes

  • spleen

  • blood

  • right lung lobe

  • subcutaneous adipose tissue

  • embryo

  • ankle joint

  • embryo

  • granulocyte
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo /QuickGO
Orthologs
SpeciesHumanMouse
Entrez

914

12481

Ensembl

ENSG00000116824

ENSMUSG00000027863

UniProt

P06729
Q53F96

P08920

RefSeq (mRNA)

NM_001767
NM_001328609

NM_013486

RefSeq (protein)

NP_001315538
NP_001758
NP_001758.2

NP_038514

Location (UCSC)Chr 1: 116.75 – 116.77 MbChr 3: 101.18 – 101.2 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
This article is about a molecule in immunology and is not to be confused with CD2, the simplified chemical formula ofdeuteratedpolyethylene.

CD2 (cluster of differentiation 2) is acell adhesion molecule found on the surface ofT cells andnatural killer (NK) cells. It has also been called T-cell surface antigen T11/Leu-5, LFA-2,[5] LFA-3 receptor, erythrocyte receptor and rosette receptor.[6]

Function

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It interacts with other adhesion molecules, such as lymphocyte function-associated antigen-3 (LFA-3/CD58) in humans, orCD48 in rodents, which are expressed on the surfaces of other cells.[7]

In addition to its adhesive properties, CD2 also acts as aco-stimulatory molecule on T and NK cells.[8]

Diagnostic relevance

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CD2 is a specific marker for T cells and NK cells, and can therefore be used inimmunohistochemistry to identify the presence of such cells in tissue sections. The great majority of T celllymphomas andleukaemias also express CD2, making it possible to use the presence of the antigen to distinguish these conditions from B cellneoplasms.[9]

Classification

[edit]

Due to its structural characteristics, CD2 is a member of theimmunoglobulin superfamily; it possesses two immunoglobulin-like domains in itsextracellular portion.[8]

Interactions

[edit]

CD2 has been shown tointeract withCD2BP2,[10]Lck[11] andPSTPIP1.[12]

References

[edit]
  1. ^abcGRCh38: Ensembl release 89: ENSG00000116824Ensembl, May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000027863Ensembl, May 2017
  3. ^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^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.Bibcode:1982PNAS...79.7489S.doi:10.1073/pnas.79.23.7489.PMC 347365.PMID 6984191.
  6. ^Uniprot database entry for CD2 (accession number P06729)
  7. ^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.
  8. ^abYang 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.
  9. ^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 978-1-84110-100-2.
  10. ^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.Bibcode:1998PNAS...9514897N.doi:10.1073/pnas.95.25.14897.PMC 24547.PMID 9843987.
  11. ^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".Journal of Experimental Medicine.183 (1):169–78.doi:10.1084/jem.183.1.169.PMC 2192399.PMID 8551220.
  12. ^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

[edit]
PDB gallery
  • 1cdb: STRUCTURE OF THE GLYCOSYLATED ADHESION DOMAIN OF HUMAN T LYMPHOCYTE GLYCOPROTEIN CD2
    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
    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
    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
    1qa9: Structure of a Heterophilic Adhesion Complex Between the Human CD2 and CD58(LFA-3) Counter-Receptors

External links

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