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Molecular architecture of mouse activating NKR-P1 receptors.

Kolenko P, Rozbeský D, Vaněk O, Kopecký V, Hofbauerová K, Novák P, Pompach P, Hašek J, Skálová T, Bezouška K, Dohnálek J
J Struct Biol 175 434-41 (2011)
Cited: 18 times
EuropePMC logo PMID: 21600988

Abstract

Receptors belonging to NKR-P1 family and their specific Clr ligands form an alternative missing self recognition system critical in immunity against tumors and viruses, elimination of tumor cells subjected to genotoxic stress, activation of T cell dependent immune response, and hypertension. The three-dimensional structure of the extracellular domain of the mouse natural killer (NK) cell receptor mNKR-P1Aex has been determined by X-ray diffraction. The core of the C-type lectin domain (CTLD) is homologous to the other CTLD receptors whereas one quarter of the domain forms an extended loop interacting tightly with a neighboring loop in the crystal. This domain swapping mechanism results in a compact interaction interface. A second dimerization interface resembles the known arrangement of other CTLD NK receptors. A functional dimeric form of the receptor is suggested, with the loop, evolutionarily conserved within this family, proposed to participate in interactions with ligands.

Articles - 3m9z mentioned but not cited (6)

  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. 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)
  3. 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)
  4. Performance of human and server prediction in CAPRI rounds 38-45. Duan R, Qiu L, Xu X, Ma Z, Merideth BR, Shyu CR, Zou X. Proteins 88 1110-1120 (2020)
  5. Structure of the H107R variant of the extracellular domain of mouse NKR-P1A at 2.3 Å resolution. Kolenko P, Rozbeský D, Vaněk O, Bezouška K, Hašek J, Dohnálek J. Acta Crystallogr Sect F Struct Biol Cryst Commun 67 1519-1523 (2011)
  6. A Hybrid Hamiltonian for the Accelerated Sampling along Experimental Restraints. Peter EK, Černý J. Int J Mol Sci 20 E370 (2019)


Reviews citing this publication (1)

  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)

Articles citing this publication (11)

  1. 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 4881-4889 (2012)
  2. Crystal structure of extracellular domain of human lectin-like transcript 1 (LLT1), the ligand for natural killer receptor-P1A. Kita S, Matsubara H, Kasai Y, Tamaoki T, Okabe Y, Fukuhara H, Kamishikiryo J, Krayukhina E, Uchiyama S, Ose T, Kuroki K, Maenaka K. Eur J Immunol 45 1605-1613 (2015)
  3. Oligomeric Architecture of Mouse Activating Nkrp1 Receptors on Living Cells. Adámková L, Kvíčalová Z, Rozbeský D, Kukačka Z, Adámek D, Cebecauer M, Novák P. Int J Mol Sci 20 E1884 (2019)
  4. Crystal structures of carbohydrate recognition domain of blood dendritic cell antigen-2 (BDCA2) reveal a common domain-swapped dimer. Nagae M, Ikeda A, Kitago Y, Matsumoto N, Yamamoto K, Yamaguchi Y. Proteins 82 1512-1518 (2014)
  5. Enhanced identification of zero-length chemical cross-links using label-free quantitation and high-resolution fragment ion spectra. Sriswasdi S, Harper SL, Tang HY, Speicher DW. J Proteome Res 13 898-914 (2014)
  6. 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)
  7. 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)
  8. 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)
  9. 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)
  10. 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)
  11. Preparation of soluble isotopically labeled NKp30, a human natural cytotoxicity receptor, for structural studies using NMR. Grave L, Tůmová L, Mrázek H, Kavan D, Chmelík J, Vaněk O, Novák P, Bezouška K. Protein Expr Purif 86 142-150 (2012)


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