Kir2dl1

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

PDB rendering based on 1b6u.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1IM9, 1NKR

Identifiers

Symbols

KIR2DL1; CD158A; KIR-K64; KIR221; NKAT; NKAT1; p58.1

External IDs

OMIM: 604936 HomoloGene: 74998 GeneCards: KIR2DL1 Gene

Gene Ontology
Molecular function	• receptor activity • protein binding
Cellular component	• plasma membrane • plasma membrane • integral to plasma membrane
Biological process	• natural killer cell inhibitory signaling pathway • immune response • regulation of immune response
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

n/a

n/a

n/a

RefSeq (mRNA)

NM_014218.2

n/a

RefSeq (protein)

NP_055033.2

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]

1 Interactions
2 See also
3 References
4 Further reading

Interactions [link]

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

References [link]

^ 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.
^ 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.
^ ^a ^b "Entrez Gene: KIR2DL1 killer cell immunoglobulin-like receptor, two domains, long cytoplasmic tail, 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3802.
^ 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. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=138585.
^ 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.
^ 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.
^ 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 [link]

Fan QR, Mosyak L, Winter CC, et al. (1997). "Structure of the inhibitory receptor for human natural killer cells resembles haematopoietic receptors". Nature 389 (6646): 96–100. DOI:10.1038/38028. PMID 9288975.
Kim J, Chwae YJ, Kim MY, et al. (1997). "Molecular basis of HLA-C recognition by p58 natural killer cell inhibitory receptors". J. Immunol. 159 (8): 3875–82. PMID 9378975.
Valiante NM, Uhrberg M, Shilling HG, et al. (1998). "Functionally and structurally distinct NK cell receptor repertoires in the peripheral blood of two human donors". Immunity 7 (6): 739–51. DOI:10.1016/S1074-7613(00)80393-3. PMID 9430220.
Uhrberg M, Valiante NM, Shum BP, et al. (1998). "Human diversity in killer cell inhibitory receptor genes". Immunity 7 (6): 753–63. DOI:10.1016/S1074-7613(00)80394-5. PMID 9430221.
Rajagopalan S, Long EO (1998). "Zinc bound to the killer cell-inhibitory receptor modulates the negative signal in human NK cells". J. Immunol. 161 (3): 1299–305. PMID 9686591.
Valés-Gómez M, Reyburn HT, Mandelboim M, Strominger JL (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.
Shilling HG, Lienert-Weidenbach K, Valiante NM, et al. (1998). "Evidence for recombination as a mechanism for KIR diversification". Immunogenetics 48 (6): 413–6. DOI:10.1007/s002510050453. PMID 9799338.
Chwae YJ, Cho SE, Kim SJ, Kim J (1999). "Diversity of the repertoire of p58 killer cell inhibitory receptors in a single individual". Immunol. Lett. 68 (2–3): 267–74. DOI:10.1016/S0165-2478(99)00062-0. PMID 10424431.
Fan QR, Wiley DC (1999). "Structure of human histocompatibility leukocyte antigen (HLA)-Cw4, a ligand for the KIR2D natural killer cell inhibitory receptor". J. Exp. Med. 190 (1): 113–23. DOI:10.1084/jem.190.1.113. PMC 2195553. PMID 10429675. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2195553.
Richardson J, Reyburn HT, Luque I, et al. (2000). "Definition of polymorphic residues on killer Ig-like receptor proteins which contribute to the HLA-C binding site". Eur. J. Immunol. 30 (5): 1480–5. DOI:10.1002/(SICI)1521-4141(200005)30:5<1480::AID-IMMU1480>3.0.CO;2-7. PMID 10820396.
Fan QR, Long EO, Wiley DC (2000). "A disulfide-linked natural killer cell receptor dimer has higher affinity for HLA-C than wild-type monomer". Eur. J. Immunol. 30 (9): 2692–7. DOI:10.1002/1521-4141(200009)30:9<2692::AID-IMMU2692>3.0.CO;2-0. PMID 11009104.
Baba E, Erskine R, Boyson JE, et al. (2001). "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.
Rajalingam R, Gardiner CM, Canavez F, et al. (2001). "Identification of seventeen novel KIR variants: fourteen of them from two non-Caucasian donors". Tissue Antigens 57 (1): 22–31. DOI:10.1034/j.1399-0039.2001.057001022.x. PMID 11169255.
Fan QR, Long EO, Wiley DC (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.
Guerra N, Michel F, Gati A, et al. (2002). "Engagement of the inhibitory receptor CD158a interrupts TCR signaling, preventing dynamic membrane reorganization in CTL/tumor cell interaction". Blood 100 (8): 2874–81. DOI:10.1182/blood-2002-02-0643. PMID 12351398.
Spaggiari GM, Contini P, Dondero A, et al. (2003). "Soluble HLA class I induces NK cell apoptosis upon the engagement of killer-activating HLA class I receptors through FasL-Fas interaction". Blood 100 (12): 4098–107. DOI:10.1182/blood-2002-04-1284. PMID 12393468.
Boyson JE, Erskine R, Whitman MC, et al. (2003). "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 138585. PMID 12454284. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=138585.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. DOI:10.1073/pnas.242603899. PMC 139241. PMID 12477932. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.

PDB gallery

1b6u: CRYSTAL STRUCTURE OF THE HUMAN KILLER CELL INHIBITORY RECEPTOR (KIR2DL3) SPECIFIC FOR HLA-CW3 RELATED ALLELES

1efx: STRUCTURE OF A COMPLEX BETWEEN THE HUMAN NATURAL KILLER CELL RECEPTOR KIR2DL2 AND A CLASS I MHC LIGAND HLA-CW3

1im9: Crystal structure of the human natural killer cell inhibitory receptor KIR2DL1 bound to its MHC ligand HLA-Cw4

1m4k: Crystal structure of the human natural killer cell activator receptor KIR2DS2 (CD158j)

1nkr: INHIBITORY RECEPTOR (P58-CL42) FOR HUMAN NATURAL KILLER CELLS

2dl2: KILLER IMMUNOGLOBULIN RECEPTOR 2DL2

2dli: KILLER IMMUNOGLOBULIN RECEPTOR 2DL2,TRIGONAL FORM

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

v t e Proteins: clusters of differentiation (see also list of human clusters of differentiation)

1-50	CD1 a-c 1A 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d CD13 CD14 CD15 CD16 A B CD18 CD19 CD20 CD21 CD22 CD23 CD24 CD25 CD26 CD27 CD28 CD29 CD30 CD31 CD32 A B CD33 CD34 CD35 CD36 CD37 CD38 CD39 CD40 CD41 CD42 a b c d CD43 CD44 CD45 CD46 CD47 CD48 CD49 a b c d e f CD50

51-100	CD51 CD52 CD53 CD54 CD55 CD56 CD57 CD58 CD59 CD61 CD62 E L P CD63 CD64 A B C CD66 a b c d e f CD68 CD69 CD70 CD71 CD72 CD73 CD74 CD78 CD79 a b CD80 CD81 CD82 CD83 CD84 CD85 a d e h j k CD86 CD87 CD88 CD89 CD90 CD91 - CD92 CD93 CD94 CD95 CD96 CD97 CD98 CD99 CD100

101-150	CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150

151-200	CD151 CD152 CD153 CD154 CD155 CD156 a b c CD157 CD158 (a d e i k) CD159 a c CD160 CD161 CD162 CD163 CD164 CD166 CD167 a b CD168 CD169 CD170 CD171 CD172 a b g CD174 CD177 CD178 CD179 a b CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200

201-250	CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 - CD248 CD249

251-300	CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299

301-350	CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350

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Contents

Interactions [link]

See also [link]

References [link]

Further reading [link]

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