The structure of the human allo-ligand HLA-B*3501 in complex with a cytochrome p450 peptide: Steric hindrance influences TCR allo-recognition

European Journal of Immunology

Volumn 36, Issue 12, 2006, Pages 3288-3293

  Hourigan, Christopher S ^a   Harkiolaki, Maria ^b   Peterson, Neil A ^b,e   Bell, John I ^c   Jones, E Yvonne ^b   O'Callaghan, Christopher A ^b,d  

^a JOHN RADCLIFFE HOSPITAL   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c University of Auckland ^*  (United Kingdom)

^d UNIVERSITY OF OXFORD   (United Kingdom)

^e UNIVERSITY OF AUCKLAND   (New Zealand)

Author keywords

Allorecognition; MHC; TCR; Transplantation

Indexed keywords

CYTOCHROME P450; HLA B35 ANTIGEN; T LYMPHOCYTE RECEPTOR;

ANTIGEN RECOGNITION; ANTIGEN STRUCTURE; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; CROSS REACTION; CRYSTAL STRUCTURE; GRAFT RECIPIENT; HLA MATCHING; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; STEREOSPECIFICITY; T LYMPHOCYTE;

AMINO ACID SEQUENCE; CRYSTALLOGRAPHY, X-RAY; CYTOCHROME P-450 ENZYME SYSTEM; HLA-B ANTIGENS; HUMANS; ISOANTIGENS; LIGANDS; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, ANTIGEN, T-CELL, ALPHA-BETA; STEREOISOMERISM;

EID: 33845587726     PISSN: 00142980     EISSN: None     Source Type: Journal    
DOI: 10.1002/eji.200636234     Document Type: Article

References (28)

1. Rocha, P. N., Plumb, T. J., Crowley, S. D. and Coffman T. M., Effector mechanisms in transplant rejection. Immunol. Rev. 2003. 196: 51-64.
2. Roelen, D. L, van Bree, S. P., van Beelen, E., Schanz, U., van Rood, J. J. and Claas, F. H., Cytotoxic T lymphocytes against HLA-B antigens are less naive than cytotoxic T lymphocytes against HLA-A antigens. Transplantation 1994. 57: 446 450.
3. van Besouw, N. M., Zuiderwijk, J. M., Vaessen, L M., Balk, A. H., Maat, A. P., van der Meide, P. H. and Weimar, W., The direct and indirect allogeneic presentation pathway during acute rejection after human cardiac transplantation. Clin. Exp. Immunol. 2005. 141: 534-540.
4. Lechler, R., Batchelor, R. and Lombardi, G., The relationship between MHC restricted and allospecific T cell recognition. Immunol. Lett. 1991. 29: 41-50.
5. Lechler, R. I., Heaton, T., Barber, L, Bal, V., Batchelor, J. R. and Lombardi, G., Molecular mimicry by major histocompatibility complex molecules and peptides accounts for some alloresponses. Immunol. Lett. 1992. 34: 63-69.
6. Burrows, S. R., Khanna R., Silins, S. L and Moss, D. J., The influence of antiviral T-cell responses on the alloreactive repertoire. Immunol. Today 1999. 20: 203-207
7. Burrows, S. R., Silins, S. L, Khanna R., Burrows, J. M., Rischmueller, M., McCluskey, J. and Moss, D. J., Cross-reactive memory T cells for Epstein-Barr virus augment the alloresponse to common human leukocyte antigens: Degenerate recognition of major histocompatibility complex-bound peptide by T cells and its role in alloreactivity. Eur. J. Immunol. 1997. 27: 1726-1736.
8. Argaet, V. P., Schmidt, C. W., Barrows, S. R., Silins, S. L, Kurilla, M. G., Doolan, D. L, Suhrbier, A. et al., Dominant selection of an invariant T cell antigen receptor in response to persistent infection by Epstein-Barr virus. J. Exp. Med. 1994.180: 2335-2340.
9. Burrows, S. R., Silins, S. L, Moss, D. J., Khanna, R., Misko, I. S. and Argaet, V. P., T cell receptor repertoire for a viral epitope in humans is diversified by tolerance to a background major histocompanbility complex antigen. J. Exp. Med. 1995. 182: 1703-1715.
10. Kjer-Nielsen, L, Clements, C. S., Brooks, A. G., Purcell, A. W., Fontes, M. R., McCluskey, J. and Rossjohn, J., The structure of HLA-B8 complexed to an immunodominant viral determinant: Peptide-induced conformational changes and a mode of MHC class I dimerization. J. Immunol. 2002. 169: 5153-5160.
11. Smith, K. J., Reid, S. W., Stuart, D. L, McMichael, A. J., Jones, E. Y. and Bell, J. I., An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501. Immunity 1996. 4: 203-213.
12. Falk, K. and Rotzschke, O., Consensus motifs and peptide ligands of MHC class I molecules. Semin. Immunol. 1993. 5: 81-94.
13. Sutton, J., Rowland-Jones, S., Rosenberg, W., Nixon, D., Gotch, F., Gao, X. M., Murray, N. et al., A sequence pattern for peptides presented to cytotoxic T lymphocytes by HLA B8 revealed by analysis of epitopes and eluted peptides. Eur. J. Immunol. 1993. 23: 447-453.
14. Kjer-Nielsen, L, Clements, C. S., Purcell, A. W., Brooks, A. G., Whisstock, J. C., Burrows, S. R., McCluskey, J. and Rossjohn, J., A structural basis for the selection of dominant alphabeta T cell receptors in antiviral immunity. Immunity 2003. 18: 53-64.
15. Borg, N. A., Ely, L. K., Beddoe, T., Macdonald, W. A., Reid, H. H., Clements, C. S., Purcell, A. W. et al., The CDR3 regions of an immunodominant T cell receptor dictate the 'energetic landscape' of peptide-MHC recognition. Nat. Immunol. 2005. 6: 171-180.
16. Reiser, J. B., Darnault, C., Gregoire, C., Mosser, T., Mazza, G., Kearney, A., van der Merwe, P. A. et al., CDR3 loop flexibility contributes to the degeneracy of TCR recognition. Nat. Immunol. 2003. 4: 241-247.
17. d peptide complexes. Immunity 1998. 8: 553-562.
18. Doxiadis, I. I., Smits, J. M., Schreuder, G. M., Persijn, G. G., van Houwelingen, H. C., van Rood, J. J. and Claas, F. H., Association between specific HLA combinations and probability of kidney allograft loss: The taboo concept. Lancet 1996. 348: 850-853.
19. Jones, E. Y., Favorite flavors of surfaces. Nat. Immunol. 2005. 6: 365-366.
20. Reid, S. W., Smith, K. J., Jakobsen, B. K., O'Callaghan, C. A., Reyburn, H., Harlos, K., Stuart, D. I. et al., Production and crystallization of MHC class I B allele single peptide complexes. FEBS Lett. 1996. 383: 119-123.
21. Otwinowski, Z. and Minor, W., Processing of X-ray diffraction data collected in oscillation mode. In Carter, C. W. and Sweet, R. K, (Eds.) Methods in Enzymology, Volume 276: Macromolecular Crystallography. Academic Press, San Diego 1997, pp 307-326.
22. Navaza, J., Implementation of molecular replacement in AMoRe. Acta Crystallogr. D Biol. Crystallogr. 2001. 57: 1367-1372.
23. Brunger, A. T., Adam, P. D., Clore, G. M., Delano, W. L, Gros, P., Grosse-Kunstleve, R. W., Jiang J. S. et al., Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 1998. 54: 905-921.
24. Jones, T. A., Zou, J. Y., Cowan, S. W. and Kjeldgaard, M., Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 1991. 47: 110-119.
25. Murshudov, G. N., Vagin, A. A. and Dodson, E. J., Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr. 1997. 53: 240-255.
26. Stuart, D. L, Levine, X, Muirhead, H. and Stammers, D. K, Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 A. J. Mol. Biol. 1979. 134: 109-142.
27. Kraulis, P., MolScript: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 1991. 24: 946-950.
28. Esnouf, R. M., An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph Model 1997. 15: 132-134.