KIR2DL1

KIR2DL1
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
Aliases KIR2DL1, CD158A, KIR-K64, KIR221, NKAT, NKAT-1, NKAT1, p58.1, killer cell immunoglobulin like receptor, two Ig domains and long cytoplasmic tail 1, KIR2DS1
External IDs HomoloGene: 130667 GeneCards: KIR2DL1
Orthologs
Species Human Mouse
Entrez

3802

n/a

Ensembl

n/a

n/a

UniProt

P43626

n/a

RefSeq (mRNA)

NM_014218

n/a

RefSeq (protein)

NP_055033.2

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Location (UCSC) Chr 19: 54.77 – 54.78 Mb n/a
PubMed search [1] n/a
Wikidata
View/Edit Human

Killer cell immunoglobulin-like receptor 2DL1 is a protein that in humans is encoded by the KIR2DL1 gene.[2][3][4]

Function

Killer-cell immunoglobulin-like receptors (KIRs) are transmembrane glycoproteins expressed by natural killer cells and subsets of T cells. The KIR genes are polymorphic and highly homologous and they are found in a cluster on chromosome 19q13.4 within the 1 Mb leukocyte receptor complex (LRC). The gene content of the KIR gene cluster varies among haplotypes, although several "framework" genes are found in all haplotypes (KIR3DL3, KIR3DP1, KIR3DL4, KIR3DL2). The KIR proteins are classified by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM), while KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals. The ligands for several KIR proteins are subsets of HLA class I molecules; thus, KIR proteins are thought to play an important role in regulation of the immune response.[4]

Interactions

KIR2DL1 has been shown to interact with HLA-C.[5][6][7][8]

See also

References

  1. ↑ "Human PubMed Reference:".
  2. ↑ Wagtmann N, Biassoni R, Cantoni C, Verdiani S, Malnati MS, Vitale M, Bottino C, Moretta L, Moretta A, Long EO (June 1995). "Molecular clones of the p58 NK cell receptor reveal immunoglobulin-related molecules with diversity in both the extra- and intracellular domains". Immunity. 2 (5): 439–49. doi:10.1016/1074-7613(95)90025-X. PMID 7749980.
  3. ↑ Colonna M, Samaridis J (May 1995). "Cloning of immunoglobulin-superfamily members associated with HLA-C and HLA-B recognition by human natural killer cells". Science. 268 (5209): 405–8. doi:10.1126/science.7716543. PMID 7716543.
  4. 1 2 "Entrez Gene: KIR2DL1 killer cell immunoglobulin-like receptor, two domains, long cytoplasmic tail, 1".
  5. ↑ Boyson JE, Erskine R, Whitman MC, Chiu M, Lau JM, Koopman LA, Valter MM, Angelisova P, Horejsi V, Strominger JL (December 2002). "Disulfide bond-mediated dimerization of HLA-G on the cell surface". Proc. Natl. Acad. Sci. U.S.A. 99 (25): 16180–5. doi:10.1073/pnas.212643199. PMC 138585Freely accessible. PMID 12454284.
  6. ↑ Baba E, Erskine R, Boyson JE, Cohen GB, Davis DM, Malik P, Mandelboim O, Reyburn HT, Strominger JL (December 2000). "N-linked carbohydrate on human leukocyte antigen-C and recognition by natural killer cell inhibitory receptors". Hum. Immunol. 61 (12): 1202–18. doi:10.1016/S0198-8859(00)00184-1. PMID 11163076.
  7. ↑ Valés-Gómez M, Reyburn HT, Mandelboim M, Strominger JL (September 1998). "Kinetics of interaction of HLA-C ligands with natural killer cell inhibitory receptors". Immunity. 9 (3): 337–44. doi:10.1016/S1074-7613(00)80616-0. PMID 9768753.
  8. ↑ Fan QR, Long EO, Wiley DC (May 2001). "Crystal structure of the human natural killer cell inhibitory receptor KIR2DL1-HLA-Cw4 complex". Nat. Immunol. 2 (5): 452–60. doi:10.1038/87766. PMID 11323700.

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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