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The interaction between natural killer (NK) cell inhibitory receptors and their cognate ligands constitutes a key mechanism by which healthy tissues are protected from NK cell-mediated lysis. However, self-ligand recognition remains poorly understood within the prototypical NKR-P1 receptor family. Here we report the structure of the inhibitory NKR-P1B receptor bound to its cognate host ligand, Clr-b. NKR-P1B and Clr-b interact via a head-to-head docking mode through an interface that includes a large array of polar interactions. NKR-P1B:Clr-b recognition is extremely sensitive to mutations at the heterodimeric interface, with most mutations severely impacting both Clr-b binding and NKR-P1B receptor function to implicate a low affinity interaction. Within the structure, two NKR-P1B:Clr-b complexes are cross-linked by a non-classic NKR-P1B homodimer, and the disruption of homodimer formation abrogates Clr-b recognition. These data provide an insight into a fundamental missing-self recognition system and suggest an avidity-based mechanism underpins NKR-P1B receptor function.

Titel:	Recognition of host Clr-b by the inhibitory NKR-P1B receptor provides a basis for missing-self recognition.
Autor/in / Beteiligte Person:	Balaji, GR ; Aguilar, OA ; Tanaka, M ; Shingu-Vazquez, MA ; Fu, Z ; Gully, BS ; Lanier, LL ; Carlyle, JR ; Rossjohn, J ; Berry, R
Link:	Full Text Finder (Volltext)
Zeitschrift:	Nature communications, Jg. 9 (2018-11-05), Heft 1, S. 4623
Veröffentlichung:	[London] : Nature Pub. Group, 2018
Medientyp:	academicJournal
ISSN:	2041-1723 (electronic)
DOI:	10.1038/s41467-018-06989-2
Schlagwort:	Animals Carrier Proteins Crystallography, X-Ray HEK293 Cells Humans Lectins, C-Type genetics Mice Mice, Inbred C57BL Models, Molecular Mutagenesis, Site-Directed Mutation NK Cell Lectin-Like Receptor Subfamily B genetics Protein Conformation Protein Conformation, alpha-Helical Protein Domains Receptors, Immunologic genetics Receptors, Natural Killer Cell genetics X-Ray Diffraction Lectins, C-Type chemistry NK Cell Lectin-Like Receptor Subfamily B chemistry Receptors, Immunologic chemistry Receptors, Natural Killer Cell chemistry
Sonstiges:	Nachgewiesen in: MEDLINE Sprachen: English Publication Type: Journal Article; Research Support, Non-U.S. Gov't Language: English [Nat Commun] 2018 Nov 05; Vol. 9 (1), pp. 4623. <i>Date of Electronic Publication: </i>2018 Nov 05. MeSH Terms: Lectins, C-Type / chemistry ; NK Cell Lectin-Like Receptor Subfamily B / chemistry ; Receptors, Immunologic / chemistry ; Receptors, Natural Killer Cell / chemistry ; Animals ; Carrier Proteins ; Crystallography, X-Ray ; HEK293 Cells ; Humans ; Lectins, C-Type / genetics ; Mice ; Mice, Inbred C57BL ; Models, Molecular ; Mutagenesis, Site-Directed ; Mutation ; NK Cell Lectin-Like Receptor Subfamily B / genetics ; Protein Conformation ; Protein Conformation, alpha-Helical ; Protein Domains ; Receptors, Immunologic / genetics ; Receptors, Natural Killer Cell / genetics ; X-Ray Diffraction References: FEBS J. 2005 Dec;272(24):6179-217. (PMID: 16336259) ; Nature. 1995 Mar 23;374(6520):327-37. (PMID: 7885471) ; J Immunol. 2015 Mar 15;194(6):2909-18. (PMID: 25681346) ; Nature. 1992 Jul 2;358(6381):66-70. (PMID: 1614533) ; Proteins. 2014 Jul;82(7):1512-8. (PMID: 24425442) ; Nat Immunol. 2003 Aug;4(8):801-7. (PMID: 12858173) ; Nat Rev Immunol. 2003 Apr;3(4):304-16. (PMID: 12669021) ; Semin Immunol. 2006 Jun;18(3):145-50. (PMID: 16740393) ; Nat Immunol. 2006 Dec;7(12):1334-42. (PMID: 17057721) ; Proc Natl Acad Sci U S A. 2004 Mar 9;101(10):3527-32. (PMID: 14990792) ; Nature. 2011 Oct 23;479(7373):401-5. (PMID: 22020283) ; Nature. 2000 Jun 1;405(6786):537-43. (PMID: 10850706) ; Cell. 2017 Mar 23;169(1):58-71.e14. (PMID: 28340350) ; Annu Rev Immunol. 2015;33:169-200. (PMID: 25493333) ; Immunogenetics. 2011 Oct;63(10):627-40. (PMID: 21667046) ; Acta Crystallogr D Biol Crystallogr. 2006 Oct;62(Pt 10):1243-50. (PMID: 17001101) ; Nature. 1998 Feb 19;391(6669):795-9. (PMID: 9486650) ; Protein Sci. 2007 Jun;16(6):1042-52. (PMID: 17473009) ; Proteins. 2016 Sep;84(9):1304-11. (PMID: 27238500) ; J Biol Chem. 2011 Jul 8;286(27):24208-18. (PMID: 21566123) ; Front Immunol. 2014 Jun 02;5:214. (PMID: 24917862) ; J Biol Chem. 2011 Jul 8;286(27):23823-30. (PMID: 21572041) ; J Immunol. 2012 Nov 15;189(10):4881-9. (PMID: 23071282) ; Int Immunol. 1994 Mar;6(3):369-76. (PMID: 8186188) ; Nat Immunol. 2012 Dec;13(12):1171-7. (PMID: 23142773) ; Annu Rev Immunol. 2005;23:225-74. (PMID: 15771571) ; J Innate Immun. 2017;9(4):343-358. (PMID: 28288457) ; Nature. 1999 Dec 9;402(6762):623-31. (PMID: 10604468) ; Nature. 1986 Feb 20-26;319(6055):675-8. (PMID: 3951539) ; J Biol Chem. 2016 Sep 2;291(36):18740-52. (PMID: 27385590) ; Proc Natl Acad Sci U S A. 2016 May 17;113(20):5682-7. (PMID: 27114505) ; J Immunol Methods. 2007 May 31;323(1):78-87. (PMID: 17433358) ; J Innate Immun. 2015;7(6):584-600. (PMID: 26044139) ; J Struct Biol. 2011 Sep;175(3):434-41. (PMID: 21600988) ; J Mol Biol. 1993 Dec 20;234(4):946-50. (PMID: 8263940) ; Nat Immunol. 2015 Nov;16(11):1153-61. (PMID: 26437244) ; Nat Immunol. 2003 Dec;4(12):1213-22. (PMID: 14595439) ; J Biol Chem. 2005 Apr 8;280(14):13593-9. (PMID: 15695803) ; Proc Natl Acad Sci U S A. 2013 Jul 9;110(28):11505-10. (PMID: 23803857) ; J Immunol. 2018 Apr 1;200(7):2231-2233. (PMID: 29555676) ; Immunity. 2000 Jun;12(6):721-7. (PMID: 10894171) ; Cancer Res. 2010 Sep 15;70(18):7102-13. (PMID: 20823164) ; Nature. 2010 Apr 8;464(7290):932-6. (PMID: 20357766) ; J Exp Med. 2008 Mar 17;205(3):725-35. (PMID: 18332182) ; Acta Crystallogr D Biol Crystallogr. 2015 Mar;71(Pt 3):578-91. (PMID: 25760607) ; Immunity. 2012 Apr 20;36(4):646-57. (PMID: 22483802) ; Nat Immunol. 2013 Jul;14(7):699-705. (PMID: 23666294) ; J Exp Med. 1998 Mar 2;187(5):813-8. (PMID: 9480992) ; Proc Natl Acad Sci U S A. 2014 Dec 9;111(49):17576-81. (PMID: 25422432) ; Immunity. 2007 May;26(5):617-27. (PMID: 17462921) ; Nat Immunol. 2007 Apr;8(4):398-408. (PMID: 17334368) ; Proc Natl Acad Sci U S A. 2010 Mar 16;107(11):5100-5. (PMID: 20194751) Grant Information: R01 AI068129 United States AI NIAID NIH HHS; 106491 International Gouvernement du Canada \| Canadian Institutes of Health Research (Instituts de Recherche en Santé du Canada); FL160100049 International Australian Research Council (ARC); APP1109901 International Department of Health \| National Health and Medical Research Council (NHMRC) Substance Nomenclature: 0 (Carrier Proteins) ; 0 (Clec2d protein, mouse) ; 0 (Lectins, C-Type) ; 0 (NK Cell Lectin-Like Receptor Subfamily B) ; 0 (Receptors, Immunologic) ; 0 (Receptors, Natural Killer Cell) Entry Date(s): Date Created: 20181107 Date Completed: 20190701 Latest Revision: 20240403 Update Code: 20240403 PubMed Central ID: PMC6218473

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Recognition of host Clr-b by the inhibitory NKR-P1B receptor provides a basis for missing-self recognition.