Leukocyte immunoglobulin-like receptor: Difference between revisions
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<StructureSection load=' | <StructureSection load='' size='350' side='right' caption='Structure of human leukocyte immunoglobulin-like receptor ligand-binding domain (salmon) complex with class I MHC (aqua), β-2 microglobulin (green) and POL polyprotein peptide (pink) (PDB entry [[1p7q]])' scene='55/552188/Cv/3'> | ||
'''Leukocyte immunoglobulin-like receptors''' (LIR) or '''CD85''' have extracellular immunoglobulin domains. LIR modulates a variety of immune cells. LIR interacts with class I MHC molecules<ref>PMID:19548123</ref>. | '''Leukocyte immunoglobulin-like receptors''' (LIR) or '''CD85''' have extracellular immunoglobulin domains. LIR modulates a variety of immune cells. LIR interacts with class I MHC molecules<ref>PMID:19548123</ref>. <scene name='55/552188/Cv/6'>Leukocyte immunoglobulin-like receptor complex with class I MHC, β-2 microglobulin and POL polyprotein peptide</scene> (PDB entry [[1p7q]]). <scene name='55/552188/Cv/7'>Interactions between LIR and class I MHC, β-2 microglobulin</scene>. | ||
*'''LILRA2''' is an activating receptor that inhibits dendritic cell differentiation. | |||
*'''LILRA5''' has a role in triggering innate immune responses. | |||
*'''LILRB1''' interacts with classical and non-classical human leukocyte antigen (HLA) class I molecules<ref>PMID:37781391</ref>. | |||
*'''LILRB3''' is a target for treatment against acute myeloid leukaemia<ref>PMID:38098451</ref>. | |||
*'''LILRB4''' suppresses immunity in solid tumors<ref>PMID:33974041</ref>. | |||
See also: | |||
*[[Immune receptors]] | |||
*[[Receptor]] | |||
</StructureSection> | </StructureSection> | ||
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{{#tree:id=OrganizedByTopic|openlevels=0| | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
* | *LILR; ligand-binding domain D1D2 27-221; ligand-binding domain D3D4 222-417 | ||
*LILRA2 subfamily A member 2 | |||
**[[2otp]] – hLILRA2 ligand-binding domain D1D2 - human<br /> | |||
*LILRA3 subfamily A member 3 | |||
**[[3q2c]] – hLILRA3 N-terminal domain <br /> | |||
*LILRA5 subfamily A member 5 | |||
**[[2d3v]] – hLILRA5 extracerllular domain <br /> | |||
**[[1vdg]] – hLILRA5 ligand-binding domain D1D2 (mutant) <br /> | |||
*LILRB1 subfamily B member 1 | |||
**[[1g0x]] – hLILRB1 ligand-binding domain D1D2<br /> | |||
**[[1ugn]] – hLILRB1 ligand-binding domain D1D2 (mutant) <br /> | |||
**[[4ll9]] – hLILRB1 ligand-binding domain D3D4 <br /> | |||
**[[7kfk]] – hLILRB1 ligand-binding domain D3D4 + Rifin<br /> | |||
**[[6zdx]] – hLILRB1 ectodomain + Rifin<br /> | |||
**[[1p7q]] – hLILRB1 ligand-binding domain D1D2 + class I MHC + β-2 microglobulin + POL polyprotein peptide<br /> | |||
**[[4no0]], [[5knm]], [[6aee]], [[6ewa]], [[6ewc]], [[6ewo]], [[6k60]] – hLILRB1 ligand-binding domain D1D2 + class I MHC + β-2 microglobulin + peptide<br /> | |||
**[[3d2u]] – hLILRB1 ligand-binding domain D1D2 + herpesvirus UL18 + β-2 microglobulin + actin peptide<br /> | |||
*LILRB2 subfamily B member 2 | |||
**[[4lla]] – hLILRB2 ligand-binding domain D3D4 <br /> | |||
**[[6aed]] – hLILRB2 ligand-binding domain D1D2D3D4 (mutant)<br /> | |||
**[[2gw5]] – hLILRB2 ligand-binding domain D1D2 <br /> | |||
**[[6bcs]] – hLILRB2 ligand-binding domain D1D2 + benzamidine<br /> | |||
**[[2dyp]] – hLILRB2 ligand-binding domain D1D2 + class I MHC + β-2 microglobulin + H2A peptide<br /> | |||
*LILRB3 subfamily B member 3 | |||
**[[6grq]], [[6grs]], [[6grt]] – mLILRB3 extracellular domain 25-619 <br /> | |||
* | *LILRB4 subfamily B member 4 | ||
* | **[[3p2t]] – hLILRB4 ligand-binding domain D1D2 <br /> | ||
**[[6k7o]] – hLILRB4 N-terminal domain + antibody <br /> | |||
}} | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Latest revision as of 12:40, 10 July 2024
Leukocyte immunoglobulin-like receptors (LIR) or CD85 have extracellular immunoglobulin domains. LIR modulates a variety of immune cells. LIR interacts with class I MHC molecules[1]. (PDB entry 1p7q). .
See also: |
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3D structures of leukocyte immunoglobulin-like receptor3D structures of leukocyte immunoglobulin-like receptor
Updated on 10-July-2024
ReferencesReferences
- ↑ Thomas R, Matthias T, Witte T. Leukocyte immunoglobulin-like receptors as new players in autoimmunity. Clin Rev Allergy Immunol. 2010 Apr;38(2-3):159-62. doi:, 10.1007/s12016-009-8148-8. PMID:19548123 doi:http://dx.doi.org/10.1007/s12016-009-8148-8
- ↑ Zeller T, Münnich IA, Windisch R, Hilger P, Schewe DM, Humpe A, Kellner C. Perspectives of targeting LILRB1 in innate and adaptive immune checkpoint therapy of cancer. Front Immunol. 2023 Sep 13;14:1240275. PMID:37781391 doi:10.3389/fimmu.2023.1240275
- ↑ Mai S, Hodges A, Chen HM, Zhang J, Wang YL, Liu Y, Nakatsu F, Wang X, Fang J, Xu Y, Davidov V, Kang K, Pingali SR, Ganguly S, Suzuki M, Konopleva M, Prinzing B, Zu Y, Gottschalk S, Lu Y, Chen SH, Pan PY. LILRB3 Modulates Acute Myeloid Leukemia Progression and Acts as an Effective Target for CAR T-cell Therapy. Cancer Res. 2023 Dec 15;83(24):4047-4062. PMID:38098451 doi:10.1158/0008-5472.CAN-22-2483
- ↑ Sharma N, Atolagbe OT, Ge Z, Allison JP. LILRB4 suppresses immunity in solid tumors and is a potential target for immunotherapy. J Exp Med. 2021 Jul 5;218(7):e20201811. PMID:33974041 doi:10.1084/jem.20201811