KIR2DL1

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Killer cell immunoglobulin-like receptor, two domains, long cytoplasmic tail, 1

PDB rendering based on 1b6u.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols KIR2DL1 ; CD158A; KIR-K64; KIR221; NKAT; NKAT1; p58.1
External IDs OMIM604936 HomoloGene130667 GeneCards: KIR2DL1 Gene
Orthologs
Species Human Mouse
Entrez 3802 n/a
Ensembl ENSG00000125498 n/a
UniProt P43626 n/a
RefSeq (mRNA) NM_014218 n/a
RefSeq (protein) NP_055033 n/a
Location (UCSC) Chr 19:
55.28 – 55.3 Mb
n/a
PubMed search [1] n/a

Killer cell immunoglobulin-like receptor 2DL1 is a protein that in humans is encoded by the KIR2DL1 gene.[1][2][3]

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.[3]

Interactions[edit]

KIR2DL1 has been shown to interact with HLA-C.[4][5][6][7]

See also[edit]

References[edit]

  1. ^ 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. 
  2. ^ 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. 
  3. ^ a b "Entrez Gene: KIR2DL1 killer cell immunoglobulin-like receptor, two domains, long cytoplasmic tail, 1". 
  4. ^ Boyson, Jonathan E; Erskine Robert, Whitman Mary C, Chiu Michael, Lau Julie M, Koopman Louise A, Valter Markus M, Angelisova Pavla, Horejsi Vaclav, Strominger Jack L (December 2002). "Disulfide bond-mediated dimerization of HLA-G on the cell surface". Proc. Natl. Acad. Sci. U.S.A. (United States) 99 (25): 16180–5. doi:10.1073/pnas.212643199. ISSN 0027-8424. PMC 138585. PMID 12454284. 
  5. ^ Baba, E; Erskine R, Boyson J E, Cohen G B, Davis D M, Malik P, Mandelboim O, Reyburn H T, Strominger J L (December 2000). "N-linked carbohydrate on human leukocyte antigen-C and recognition by natural killer cell inhibitory receptors". Hum. Immunol. (United States) 61 (12): 1202–18. doi:10.1016/S0198-8859(00)00184-1. ISSN 0198-8859. PMID 11163076. 
  6. ^ Valés-Gómez, M; Reyburn H T, Mandelboim M, Strominger J L (September 1998). "Kinetics of interaction of HLA-C ligands with natural killer cell inhibitory receptors". Immunity (UNITED STATES) 9 (3): 337–44. doi:10.1016/S1074-7613(00)80616-0. ISSN 1074-7613. PMID 9768753. 
  7. ^ Fan, Q R; Long E O, Wiley D C (May 2001). "Crystal structure of the human natural killer cell inhibitory receptor KIR2DL1-HLA-Cw4 complex". Nat. Immunol. (United States) 2 (5): 452–60. doi:10.1038/87766. ISSN 1529-2908. PMID 11323700. 

Further reading[edit]

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