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Mouse Clr-g, a ligand for NK cell activation receptor NKR-P1F: crystal structure and biophysical properties.

Skálová T, Kotýnková K, Dušková J, Hašek J, Koval T, Kolenko P, Novák P, Man P, Hanč P, Vaněk O, Bezouška K, Dohnálek J
J Immunol 189 4881-9 (2012)
Cited: 15 times
EuropePMC logo PMID: 23071282

Abstract

Interactions between C-type lectin-like NK cell receptors and their protein ligands form one of the key recognition mechanisms of the innate immune system that is involved in the elimination of cells that have been malignantly transformed, virally infected, or stressed by chemotherapy or other factors. We determined an x-ray structure for the extracellular domain of mouse C-type lectin related (Clr) protein g, a ligand for the activation receptor NKR-P1F. Clr-g forms dimers in the crystal structure resembling those of human CD69. This newly reported structure, together with the previously determined structure of mouse receptor NKR-P1A, allowed the modeling and calculations of electrostatic profiles for other closely related receptors and ligands. Despite the high similarity among Clr-g, Clr-b, and human CD69, these molecules have fundamentally different electrostatics, with distinct polarization of Clr-g. The electrostatic profile of NKR-P1F is complementary to that of Clr-g, which suggests a plausible interaction mechanism based on contacts between surface sites of opposite potential.

Articles - 3rs1 mentioned but not cited (3)

  1. Recognition of host Clr-b by the inhibitory NKR-P1B receptor provides a basis for missing-self recognition. Balaji GR, Aguilar OA, Tanaka M, Shingu-Vazquez MA, Fu Z, Gully BS, Lanier LL, Carlyle JR, Rossjohn J, Berry R. Nat Commun 9 4623 (2018)
  2. Four crystal structures of human LLT1, a ligand of human NKR-P1, in varied glycosylation and oligomerization states. Skálová T, Bláha J, Harlos K, Dušková J, Koval' T, Stránský J, Hašek J, Vaněk O, Dohnálek J. Acta Crystallogr D Biol Crystallogr 71 578-591 (2015)
  3. Production of recombinant soluble dimeric C-type lectin-like receptors of rat natural killer cells. Vaněk O, Celadova P, Skořepa O, Bláha J, Kalousková B, Dvorská A, Poláchová E, Pucholtová H, Kavan D, Pompach P, Hofbauerová K, Kopecký V, Mesci A, Voigt S, Carlyle JR. Sci Rep 9 17836 (2019)


Reviews citing this publication (2)

  1. Modulation of NK cell function by genetically coupled C-type lectin-like receptor/ligand pairs encoded in the human natural killer gene complex. Bartel Y, Bauer B, Steinle A. Front Immunol 4 362 (2013)
  2. Complexity and Diversity of the NKR-P1:Clr (Klrb1:Clec2) Recognition Systems. Kirkham CL, Carlyle JR. Front Immunol 5 214 (2014)

Articles citing this publication (10)

  1. Structure of NKp65 bound to its keratinocyte ligand reveals basis for genetically linked recognition in natural killer gene complex. Li Y, Wang Q, Chen S, Brown PH, Mariuzza RA. Proc Natl Acad Sci U S A 110 11505-11510 (2013)
  2. Clr-a: A Novel Immune-Related C-Type Lectin-like Molecule Exclusively Expressed by Mouse Gut Epithelium. Rutkowski E, Leibelt S, Born C, Friede ME, Bauer S, Weil S, Koch J, Steinle A. J Immunol 198 916-926 (2017)
  3. Nkrp1 family, from lectins to protein interacting molecules. Rozbeský D, Ivanova L, Hernychová L, Grobárová V, Novák P, Černý J. Molecules 20 3463-3478 (2015)
  4. OCILRP2 signaling synergizes with LPS to induce the maturation and differentiation of murine dendritic cells. Chai L, Wu S, Liu G, Wang Z, Tian W, Ma Y. Biochem Biophys Res Commun 446 836-842 (2014)
  5. Re-evaluation of the involvement of NK cells and C-type lectin-like NK receptors in modulation of immune responses by multivalent GlcNAc-terminated oligosaccharides. Grobárová V, Benson V, Rozbeský D, Novák P, Cerný J. Immunol Lett 156 110-117 (2013)
  6. Solution structure of the lymphocyte receptor Nkrp1a reveals a distinct conformation of the long loop region as compared to in the crystal structure. Rozbeský D, Adámek D, Pospíšilová E, Novák P, Chmelík J. Proteins 84 1304-1311 (2016)
  7. Structure of the human NK cell NKR-P1:LLT1 receptor:ligand complex reveals clustering in the immune synapse. Bláha J, Skálová T, Kalousková B, Skořepa O, Cmunt D, Grobárová V, Pazicky S, Poláchová E, Abreu C, Stránský J, Kovaľ T, Dušková J, Zhao Y, Harlos K, Hašek J, Dohnálek J, Vaněk O. Nat Commun 13 5022 (2022)
  8. A Hybrid Hamiltonian for the Accelerated Sampling along Experimental Restraints. Peter EK, Černý J. Int J Mol Sci 20 E370 (2019)
  9. Mouse Ocilrp2/Clec2i negatively regulates LPS-mediated IL-6 production by blocking Dap12-Syk interaction in macrophage. Cao M, Ma L, Yan C, Wang H, Ran M, Chen Y, Wang X, Liang X, Chai L, Li X. Front Immunol 13 984520 (2022)
  10. Tumor Marker B7-H6 Bound to the Coiled Coil Peptide-Polymer Conjugate Enables Targeted Therapy by Activating Human Natural Killer Cells. Kalousková B, Skořepa O, Cmunt D, Abreu C, Krejčová K, Bláha J, Sieglová I, Král V, Fábry M, Pola R, Pechar M, Vaněk O. Biomedicines 9 1597 (2021)


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