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Variable MHC class I engagement by Ly49 natural killer cell receptors demonstrated by the crystal structure of Ly49C bound to H-2K(b).

Dam J, Guan R, Natarajan K, Dimasi N, Chlewicki LK, Kranz DM, Schuck P, Margulies DH, Mariuzza RA
Nat Immunol 4 1213-22 (2003)
Cited: 86 times
EuropePMC logo PMID: 14595439

Abstract

The Ly49 family of natural killer (NK) receptors regulates NK cell function by sensing major histocompatibility complex (MHC) class I. Ly49 receptors show complex patterns of MHC class I cross-reactivity and, in certain cases, peptide selectivity. To investigate whether specificity differences result from topological differences in MHC class I engagement, we determined the structure of the peptide-selective receptor Ly49C in complex with H-2K(b). The Ly49C homodimer binds two MHC class I molecules in symmetrical way, a mode distinct from that of Ly49A, which binds MHC class I asymmetrically. Ly49C does not directly contact the MHC-bound peptide. In addition, MHC crosslinking by Ly49C was demonstrated in solution. We propose a dynamic model for Ly49-MHC class I interactions involving conformational changes in the receptor, whereby variations in Ly49 dimerization mediate different MHC-binding modes.

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  1. NK cell recognition. Lanier LL. Annu Rev Immunol 23 225-274 (2005)
  2. Controlling natural killer cell responses: integration of signals for activation and inhibition. Long EO, Kim HS, Liu D, Peterson ME, Rajagopalan S. Annu Rev Immunol 31 227-258 (2013)
  3. The C-type lectin-like domain superfamily. Zelensky AN, Gready JE. FEBS J 272 6179-6217 (2005)
  4. The Molecular Mechanism of Natural Killer Cells Function and Its Importance in Cancer Immunotherapy. Paul S, Lal G. Front Immunol 8 1124 (2017)
  5. Activating and inhibitory receptors of natural killer cells. Pegram HJ, Andrews DM, Smyth MJ, Darcy PK, Kershaw MH. Immunol Cell Biol 89 216-224 (2011)
  6. A decade of yeast surface display technology: where are we now? Pepper LR, Cho YK, Boder ET, Shusta EV. Comb Chem High Throughput Screen 11 127-134 (2008)
  7. Cis interactions of immunoreceptors with MHC and non-MHC ligands. Held W, Mariuzza RA. Nat Rev Immunol 8 269-278 (2008)
  8. The regulation of lymphocyte activation by inhibitory receptors. Leibson PJ. Curr Opin Immunol 16 328-336 (2004)
  9. Structural and dynamic control of T-cell receptor specificity, cross-reactivity, and binding mechanism. Baker BM, Scott DR, Blevins SJ, Hawse WF. Immunol Rev 250 10-31 (2012)
  10. 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)
  11. Tapasin and other chaperones: models of the MHC class I loading complex. Wright CA, Kozik P, Zacharias M, Springer S. Biol Chem 385 763-778 (2004)
  12. Structural basis for recognition of MHC and MHC-like ligands by natural killer cell receptors. Deng L, Mariuzza RA. Semin Immunol 18 159-166 (2006)
  13. Survey of the year 2003 commercial optical biosensor literature. Rich RL, Myszka DG. J Mol Recognit 18 1-39 (2005)
  14. Structural basis for recognition of cellular and viral ligands by NK cell receptors. Li Y, Mariuzza RA. Front Immunol 5 123 (2014)
  15. Complexity and Diversity of the NKR-P1:Clr (Klrb1:Clec2) Recognition Systems. Kirkham CL, Carlyle JR. Front Immunol 5 214 (2014)
  16. Peptide and Peptide-Dependent Motions in MHC Proteins: Immunological Implications and Biophysical Underpinnings. Ayres CM, Corcelli SA, Baker BM. Front Immunol 8 935 (2017)
  17. Structural and functional aspects of the Ly49 natural killer cell receptors. Dimasi N, Biassoni R. Immunol Cell Biol 83 1-8 (2005)
  18. How the virus outsmarts the host: function and structure of cytomegalovirus MHC-I-like molecules in the evasion of natural killer cell surveillance. Revilleza MJ, Wang R, Mans J, Hong M, Natarajan K, Margulies DH. J Biomed Biotechnol 2011 724607 (2011)
  19. The balancing act: inhibitory Ly49 regulate NKG2D-mediated NK cell functions. Malarkannan S. Semin Immunol 18 186-192 (2006)
  20. Structure of the Ly49 family of natural killer (NK) cell receptors and their interaction with MHC class I molecules. Dimasi N, Moretta L, Biassoni R. Immunol Res 30 95-104 (2004)
  21. NK cell receptors and their MHC class I ligands in host response to cytomegalovirus: insights from the mouse genome. Pyzik M, Kielczewska A, Vidal SM. Semin Immunol 20 331-342 (2008)
  22. The Ly49 natural killer cell receptors: a versatile tool for viral self-discrimination. Berry R, Rossjohn J, Brooks AG. Immunol Cell Biol 92 214-220 (2014)
  23. Structural Models for Roseolovirus U20 And U21: Non-Classical MHC-I Like Proteins From HHV-6A, HHV-6B, and HHV-7. Weaver GC, Arya R, Schneider CL, Hudson AW, Stern LJ. Front Immunol 13 864898 (2022)
  24. Inflammatory-driven NK cell maturation and its impact on pathology. Bourayou E, Golub R. Front Immunol 13 1061959 (2022)

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