Crystal structure of an NK cell immunoglobulin-like receptor in complex with its class I MHC ligand

Nature

Volumn 405, Issue 6786, 2000, Pages 537-543

  Boylngton, Jeffrey C ^a   Motykat, Shawn A ^b   Schuckt, Peter ^c   Brooks, Andrew G ^d   Sun, Peter D ^a  

^a NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES   (United States)

^b JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c NATIONAL INSTITUTES OF HEALTH   (United States)

^d UNIVERSITY OF MELBOURNE   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

HLA ANTIGEN; IMMUNOGLOBULIN RECEPTOR; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; T LYMPHOCYTE RECEPTOR;

ALPHA HELIX; ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; GENE MUTATION; HYDROGEN BOND; LIGAND BINDING; NATURAL KILLER CELL; PRIORITY JOURNAL; PROTEIN BINDING; TARGET CELL DESTRUCTION;

AMINO ACID SEQUENCE; CRYSTALLOGRAPHY, X-RAY; ELECTROCHEMISTRY; ESCHERICHIA COLI; HLA-C ANTIGENS; HUMANS; KILLER CELLS, NATURAL; LIGANDS; MAJOR HISTOCOMPATIBILITY COMPLEX; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN CONFORMATION; RECEPTOR AGGREGATION; RECEPTORS, ANTIGEN, T-CELL; RECEPTORS, IMMUNOLOGIC; RECOMBINANT PROTEINS;

EID: 0034213423     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35014520     Document Type: Article

References (43)

1. Biron, C. A., Nguyen, K. B., Pien, G. C., Cousens, L. P. & Salazar-Mather, T. P. Natural killer cells in antiviral defense: function and regLlatiun by innate cytokines. Anno. Rev. Immonol. 17, 189-220 (1999).
2. Lanier, L. L. NK cell receptors. Annu. Rev. Immunol 16, 359-393 (1998).
3. Lanier, L. L., Corliss, B. C., Wu, J., Leong, C. & Phillips, J. H. Immunoreceptor DAP12 bearing a lyrosine-based activation motif is invovled in activating NK cells. Nature 391, 703-707 (1998).
4. Long, E. O. Regulation of immune responses through inhibitory receptors. Annu. Rev. Immunol. 17, 875-904 (1999).
5. Pende, D. et al. The susceptibility to natural killer cell-mediated lysis of HLA class 1-positive melanomas reflects the expression of insufficient amounts of different HLA class I alleles. Eur. J. Immunol. 28, 2384-2394 (1998).
6. Fan, Q. R. et al. Structure of the inhibitory receptor for human natural killer cells resembles haematopoietic receptors. Nature 389, 96-100 (1997).
7. Snyder, G. A., Brooks, A. G. & Sun, P. D. Crystal structure of the HLA-Cw3 allotype-specific killer cell inhibitory receptor KIR2DL2. Proc. Natl Acad. Sci. USA 96, 3864-3869 (1999).
8. Maenaka, K., Juji, T., Stuart, D. I. & Jones, E. Y. Crystal structure of the human p58 killer cell inhibitory receptor (KIR2DL3) specific for HLA-Cw3-related MHC class I. Structure 7, 391-398 (1999).
9. Boyington, J. C. et al. Structure of CD94 reveals a novel C-type lectin fold: implications for the NK cell-associated CD94/NKG2 receptors. Immunity 10, 75-82 (1999).
10. Tormo, J., Natarajan, K., Margulies, D. H. & Mariuzza, R. A. Crystal structure of a lectin-like natural killer cell receptor bound to its MHC, class I ligand. Nature 402, 623-631 (1999).
11. Winter, C. C., Gumperz, J. E., Parham, P., Long, E. O. & Wagttmann, N. Direct binding and functional transfer of NK cell inhibitory receptors reveal novel patterns of HLA-C allotype recognition. J. Immunol. 161, 571-577 (1998).
12. Winter, C., C. & Long, E. O. A single amino acid in the p58 killer cell inhibitory receptors contorls the ability of natural killer cells to discriminate between the two groups of HLA-C allotypes. J. Immunol. 158, 4026-4028 (1997).
13. Biassoni, R. et al. Role of amino acid position 70 in the binding affinity of p50.1 and p58.1 receptors for HLA-Cw4 molecules. Eur. J. Immunol. 27, 3095-3099 (1997).
14. Fan, Q R. & Wiley, D. C. Structure of human histocompatibility leukocyte antigen (HLA)-Cw4, a ligand for the KIR2D natural killer cell inhibitory receptor J. Exp. Mol. 190, 113-123 (1999).
15. Lawrence, M. C. & Colman, P. M. Shape complementarity at protein/protein interfaces. J. Mol. Biol. 234, 946-950 (1993).
16. Ysern, X., Li, H. & Mariuzza, R. A. Imperfect interfaces. Nature Struct. Biol. 5, 412-414 (1998).
17. Wang, J. H. et al. Structure of a heterophilic adhesion complex between the human CD2 and CD58 (LFA-3) counterreceptors. Cell 97, 791-803 (1999).
18. Mandelboim, O. et al. The binding site of NK receptors on HLA-C molecules. Immunity 6, 341-350 (1997).
19. + 0304 confer different degrees of protection from natural killer cell-mediated lysis. Proc. Natl Acad. Sci. USA 94, 6313-6318 (1997).
20. Falk, K. et al. Allele-specific peptide ligand motifs of HLA-C molecules. Proc. Natl Acad. Sci. USA 90, 12005-12009 (1993).
21. Garboczi, D. N. et al. Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. Nature 384, 134-141 (1996).
22. Rajagopalan, S. & Long, E. O. The direct binding of a p58 killer cell inhibitory receptor to human histocompatibility leukocyte antigen (HLA)-Cw4 exhibits peptide selectivity J. Exp. Med. 185, 1523-1528 (1997).
23. Vales-Gomez, M., Reyburn, H. T., Erskine, R. A. & Strominger, J. Differential binding to HLA-C of p50-activating and p58-inhibitory natural killer cell receptors. Proc. Natl Acad. Sci. USA 95, 14326-14331 (1998).
24. Maenak, K. et al. Killer cell immunoglobulin receptors and T cell receptor bind peptide-major histocompatibility complex class I wiht distinct thermodynamic and kinetic properties. J. Biol. Chem. 274, 28329-28334 (1999).
25. Davis, S. J., Ikemizu, ,S., Wild, M. K. & van der Merwe, P. A. CD2 and the nature of protein interactions mediating cell-cell recognition. Immunol Rev. 163, 217-236 (1998).
26. Colonna, M., Borsellino, G., Falco, M., Ferrara, G. B. & Strominger, J. L. HLA-C is the inhibitory ligand that determines dominant resistance to lysis by NK1-and NK2-specific natural killer cells. Proc. Natl Acad. Sci. USA 90, 12000-12004 (1993).
27. Mandelboim, O. et al. Protection from lysis by natural killer cells of group 1 and 2 specificity is mediated by residue 80 in human histocompatibility leukocyte antigen C alleles and also occurs with empty major histocompatibility complex molecules. J. Exp. Med. 184, 913-922 (1996).
28. +4601 has high selectivity in peptide binding and functions characteristic of HLA-C. J. Exp. Med. 184, 735-740 (1996).
29. +2705 by specific natural killer cells. J. Immunol. 157, 3350-3336 (1996).
30. +5101: requirement for all three p70 immunoglobulin domains. Eur. J. Immunol. 27, 568-571 (1997).
31. Littaua, R. A. et al. An HLA-C-restricted CD8+ cytoxic T-lymphocyte clone recognizes a highly conserved epitope on human immunodeficiency virus type I gag. J. Virol. 65, 4051-4056 (1991).
32. Hanke, T. et al. Direct assessment of MHC class I binding by seven Ly49 inhibitory NK cell receptors. Immunity 11, 67-77 (1999).
33. Orihuela, M., Margulies D. H. & Yokoyama, W. M. The natural killer cell receptor Ly-49A recognizes a peptide-induced conformational determinant on its major histocompatibility complex class I ligand. Proc. Natl Acad. Sci. USA 93, 11792-11797 (1996).
34. Rajagopalan, S., Winter, C. C., Wagtmann, N. & Long, E. O. The Ig-related killer cell inhibitory receptor binds zinc and requires zinc for recognition of HLA-C on target cells. J. Immunol. 155, 4143-4146 (1995).
35. Davis, D. M. et al. The human natural killer cell immune synapse. Proc. Natl Acad. Sci. USA 96, 15062-15067 (1999).
36. Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
37. Navaza, J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50, 157-163 (1994).
38. Brunger, A. T. et al. Crystallography & NMR system: A Software Suite for Macromolecular Structure Determination. Acta Crystallogr. D 54, 905-921 (1998).
39. Jones, T. A., Zou, J. Y., Cowan, S. w. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in the models. Acta Crystallogr. A 47, 110-119 (1991).
40. The Collaborative Computing Project No. 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1995).
41. Kraulis, P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Applied Crystallography 24, 946-950 (1991).
42. Merrit, E. A. & Murphy, M. E. P. Raster 3D Version 2.0: a program for photorealistic molecular graphics. Acta Crystallogr. D 50, 869-873 (1994).
43. Nicholls, A., Charp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11, 281-296 (1991).