Biology:KIR2DS4

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Short description: Protein-coding gene in the species Homo sapiens

A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Killer cell immunoglobulin-like receptor 2DS4 is a protein that in humans is encoded by the KIR2DS4 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 (DAP12) 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]

KIR2DS4 is a product of a gene conversion with KIR3DL2.[4] KIR2DS4 has unusual HLA-I specificity binding some HLA-C allotypes and HLA-A*11.[4] A common allele of KIR2DS4 encodes a truncated version (KIR-1D) that has no HLA-I binding ability.[4][5] Recent evidence suggests KIR2DS4 detects HLA-C presented peptides in a peptide-specific manner, detecting peptides conserved in bacteria.[6][7][8]

See also

References

  1. "A novel surface molecule homologous to the p58/p50 family of receptors is selectively expressed on a subset of human natural killer cells and induces both triggering of cell functions and proliferation". European Journal of Immunology 26 (8): 1816–1824. August 1996. doi:10.1002/eji.1830260823. PMID 8765026. 
  2. "Molecular clones of the p58 NK cell receptor reveal immunoglobulin-related molecules with diversity in both the extra- and intracellular domains". Immunity 2 (5): 439–449. May 1995. doi:10.1016/1074-7613(95)90025-X. PMID 7749980. 
  3. 3.0 3.1 "Entrez Gene: KIR2DS4 killer cell immunoglobulin-like receptor, two domains, short cytoplasmic tail, 4". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=3809. 
  4. 4.0 4.1 4.2 "KIR2DS4 is a product of gene conversion with KIR3DL2 that introduced specificity for HLA-A*11 while diminishing avidity for HLA-C". The Journal of Experimental Medicine 206 (11): 2557–2572. October 2009. doi:10.1084/jem.20091010. PMID 19858347. 
  5. "Studies on the expression of the deleted KIR2DS4*003 gene product and distribution of KIR2DS4 deleted and nondeleted versions in different populations". Human Immunology 68 (2): 128–134. February 2007. doi:10.1016/j.humimm.2006.12.007. PMID 17321903. 
  6. "Human NK cell receptor KIR2DS4 detects a conserved bacterial epitope presented by HLA-C". Proceedings of the National Academy of Sciences of the United States of America 116 (26): 12964–12973. June 2019. doi:10.1073/pnas.1903781116. PMID 31138701. Bibcode2019PNAS..11612964S. 
  7. "A natural killer cell receptor takes sharp aim at the world of bacteria". Proceedings of the National Academy of Sciences of the United States of America 116 (26): 12601–12603. June 2019. doi:10.1073/pnas.1907937116. PMID 31175150. Bibcode2019PNAS..11612601P. 
  8. "Innate receptors with high specificity for HLA class I-peptide complexes". Science Immunology 8 (87). September 2023. doi:10.1126/sciimmunol.adh1781. PMID 37683038. 

Further reading

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