CD2

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CD2 molecule
CD2 antigen.png
The protein structure of CD2. From PDB 1hnf
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols CD2 ; LFA-2; SRBC; T11
External IDs OMIM186990 MGI88320 HomoloGene1338 ChEMBL: 2040 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 P08920
RefSeq (mRNA) NM_001767 NM_013486
RefSeq (protein) NP_001758 NP_038514
Location (UCSC) Chr 1:
117.3 – 117.31 Mb
Chr 3:
101.28 – 101.29 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,[1] LFA-3 receptor, erythrocyte receptor and rosette receptor.[2]


Function[edit]

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[edit]

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[edit]

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[edit]

CD2 has been shown to interact with CD2BP2,[6] Lck[7] and PSTPIP1.[8]

References[edit]

  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: 7489. doi:10.1073/pnas.79.23.7489. PMID 6984191. 
  2. ^ Uniprot database entry for CD2 (accession number P06729)
  3. ^ 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. 
  4. ^ 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. 
  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 E L (December 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. 
  7. ^ Bell, G M; Fargnoli J; Bolen J B; Kish L; Imboden J B (January 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. 
  8. ^ Li, J; Nishizawa K; An W; Hussey R E; Lialios F E; Salgia R; Sunder-Plassmann R; Reinherz E L (December 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. 

Further reading[edit]

External links[edit]