Structural basis of 2C TCR allorecognition of H-2L(d) peptide complexes

Immunity

Volumn 8, Issue 5, 1998, Pages 553-562

  Speir, Jeffrey A ^a   Garcia, K Christopher ^a   Brunmark, Anders ^b   Degano, Massimo ^a   Peterson, Per A ^b   Teyton, Luc ^a   Wilson, Ian A ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b GENERAL ATOMICS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

H2 ANTIGEN; T LYMPHOCYTE RECEPTOR;

ALLOIMMUNITY; ANTIGEN PRESENTATION; ANTIGEN RECOGNITION; ARTICLE; CRYSTAL STRUCTURE; PRIORITY JOURNAL;

EID: 0032076119     PISSN: 10747613     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-7613(00)80560-9     Document Type: Article

References (78)

1. al-Ramadi, B.K., Jelonek, M.T., Boyd, L.F., Margulies, D.H., and Bothwell, A.L. (1995). Lack of strict correlation of functional sensitization with the apparent affinity of MHC/peptide complexes for the TCR. J. Immunol. 155, 662-673.
2. Arden, B., Clark, S.P., Kabelitz, D., and Mak, T.W. (1995). Mouse T-cell receptorvariable gene segment families, Immunogenetics 42, 501-530.
3. Bacon, D.J., and Anderson, W.F. (1988). Raster3D. J. Mol. Graph. 6, 219-220.
4. d with β2-microglobulin and peptide. Proc. Natl. Acad. Sci. USA 94, 6880-6885.
5. d are influenced by its amino terminus. J. Immunol. 137, 916-923.
6. Bjorkman, P.J., Saper, M.A., Samraoui, B., Bennett, W.S., Strominger, J.L., and Wiley, D.C. (1987). Structure of the human class I histocompatibility antigen, HLA-A2. Nature 329, 506-512.
7. Bouvier, M., and Wiley, D.C. (1994). Importance of peptide amino and carboxyl termini to the stability of MHC class I molecules. Science 265, 398-402.
8. Brock, R.,Wiesmuller, K.H., Jung, G., and Walden, P. (1996). Molecular basis for the recognition of two structurally different histocompatibility complex/peptide complexes by a single T-cell receptor. Proc. Natl. Acad. Sci. USA 93, 13108-13113.
9. Brünger, A.T. (1997). The free R value: a more objective statistic for crystallography. Meth. Enzymol. 277, 366-396.
10. Brünger, A.T., Kuriyan, J., and Karplus, M. (1987). Crystallographic R factor refinement by molecular dynamics. Science 235, 458-460.
11. Clackson, T., and Wells, J.A. (1995). A hot spot of binding energy in a hormone-receptor interface. Science 267, 383-386.
12. - strains. Proc. Natl. Acad. Sci. USA 91, 11482-11486.
13. Connolly, M.L. (1983). Solvent-accessible surfaces of proteins and nucleic acids. Science 221, 709-713.
14. Corr, M., Slanetz, A.E., Boyd, L.F., Jelonek, M.T., Khilko, S., al-Ramadi, B.K., Kim, Y.S., Mäher, S.E., Bothwell, A.L., and Margulies, D.H. (1994). Tcell receptor-MHC class I peptide interactions: affinity, kinetics, and specificity. Science 265, 946-949.
15. Dodson, E., Kleywegt, G.J., and Wilson, K. (1996). Report of a workshop on the use of statistical validators in protein x-ray crystallography. Acta Cryst. D52, 228-234.
16. Dutz, J.P., Tsomides, T.J., Kageyama, S., Rasmussen, M.H., and Eisen, H.N. (1994). A cytotoxic T lymphocyte clone can recognize the same naturally occurring self peptide in association with a self and nonself class I MHC protein. Mol. Immunol. 31, 967-975.
17. Eisen, H.N., Sykulev, Y., and Tsomides, T.J. (1996). Antigen-specific T-cell receptors and their reactions with complexes formed by peptides with major histocompatibility complex proteins. Adv. Protein Chem. 49, 1-56.
18. Ferrin, T.E., Huang, C.C., Jarvis, L.E., and Langridge, R. (1988). The MIDAS display system. J. Mol. Graph. 6, 13-27.
19. b. Science 257, 919-927.
20. b-ovalbumin peptide complex reveals the interplay of primary and secondary anchor positions in the major histocompatibility complex binding groove. Proc. Natl. Acad. Sci. USA 92, 2479-2483.
21. Garboczi, D.N., Ghosh, P., Utz, U., Fan, Q.R., Biddison, W.E., and Wiley, D.C. (1996). Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. Nature 384, 134-141.
22. Garcia, K.C., Degano, M., Stanfield, R.L., Brunmark, A., Jackson, M.R., Peterson, P.A., Teyton, L., and Wilson, I.A. (1996). An αβ T cell receptor structure at 2.5 Å and its orientation in the TCR-MHC complex. Science 274, 209-219.
23. Garcia, K.C., Tallquist, M.D., Pease, L.R., Brunmark, A., Scott, C.A., Degano, M., Stura, E.A., Peterson, P.A., Wilson, I.A., and Teyton, L. (1997). αβ T-cell receptor interactions with syngeneic and allogeneic ligands: affinity measurements and crystallization. Proc. Natl. Acad. Sci. USA 94, 13838-13843.
24. Garcia, K.C., Degano, M., Pease, L.R., Huang, M., Peterson, P.A., Teyton, L., and Wilson, I.A. (1998). Structural basis of plasticity in T-cell receptor recognition of a self peptide-MHC antigen. Science 279, 1166-1172.
25. Garrett, T.P., Saper, M.A., Bjorkman, P.J., Strominger, J.L., and Wiley, D.C. (1989). Specificity pockets for the side chains of peptide antigens in HLA-Aw68. Nature 342, 692-696.
26. Germain, R.N. (1990). Immunology. Making a molecular match. Nature 344, 19-22.
27. Gillanders, W.E., Hanson, H.L., Rubocki, RJ., Hansen, T.H., and Connolly, J.M. (1997). Class I-restricted cytotoxic T cell recognition of split peptide ligands. Int. Immunol. 9, 81-89.
28. Harrison, S.C. (1968). A point-focusing camera for single-crystal diffraction. J. Appl. Cryst. 1, 84-90.
29. Haskins, K., Kappler, J., and Marrack, P. (1984). The major histocompatibility complex-restricted antigen receptor on T cells. Annu. Rev. lmmunol. 2, 51-66.
30. Holm, L., and Sander, C. (1993). Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138.
31. Hong, S.C., Chelouche, A., Lin, R.H., Shaywitz, D., Braunstein, N.S., Glimcher, L., and Janeway, C.A., Jr. (1992). An MHC interaction site maps to the amino-terminal half of the T cell receptor a-chain variable domain. Cell 69, 999-1009.
32. Hutchinson, E.G., and Thornton, J.M. (1996). PROMOTIF: a program to identify and analyze structural motifs in proteins. Protein Sci. 5, 212-220.
33. Jackson, M.R., Song, E.S., Yang, Y., and Peterson, P.A. (1992). Empty and peptide-containing conformers of class I major histocompatibility complex molecules expressed in Drosophila melanogaster cells. Proc. Natl. Acad. Sci. USA 89, 12117-12121.
34. Jameson, S.C., Hogquist, K.A., and Bevan, M.J. (1995). Positive selection of thymocytes. Annu. Rev. Immunol. 13, 93-126.
35. Jones, T.A., Cowan, S., Zou, J.Y., and Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A47, 110-119.
36. Kabsch, W. (1988). Evaluation of single crystal x-ray diffraction data from a position sensitive detector. J. Appl. Cryst. 21, 916-924.
37. Klein, J. (1986). Natural History of the Major Histocompatibility Complex (New York: John Wiley and Sons).
38. Kleywegt, G.J., and Brünger, A.T. (1996). Checking your imagination: applications of the free R value. Structure 4, 897-904.
39. Kleywegt, G.J., and Jones, T.A. (1997). Model building and refinement practice. Meth. Enzymol. 277, 208-230.
40. Kraulis, P.J. (1991). MOLSCRIPT. J. Appl. Cryst. 24, 946-950.
41. Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.
42. Livnah, O., Stura, E.A., Johnson, D.L., Middleton, S.A., Mulcahy, L.S., Wrighton, N.C., Dower, W.J., Jolliffe, L.K., and Wilson, I.A. (1996). Functional mimicry of a protein hormone by a peptide agonist: the EPO receptor complex at 2.8 Å. Science 273, 464-471.
43. Manning, T.C., Schlueter, C.J., Brodnicki, T.C., Parke, E.A., Speir, J.A., Garcia, K.C., Teyton, L., Wilson, I.A., and Kranz, D.M. (1998). Alanine scanning mutagenesis of an αβ T cell receptor: mapping the energy of antigen recognition. Immunity 8, 413-425.
44. Matsumura, M., Saito, Y., Jackson, M.R., Song, E.S., and Peterson, P.A. (1992). In vitro peptide binding to soluble empty class I major histocompatibility complex molecules isolated from transfected Drosophila melanogastercells. J. Biol. Chem. 267, 23589-23595.
45. Matthews, B.W. (1968). Solvent content of protein crystals. J. Mol. Biol. 33, 491-497.
46. McCoy, A.J., Chandana-Epa, V., and Colman, P.M. (1997). Electrostatic complementarity at protein/protein interfaces. J. Mol. Biol. 268, 570-584.
47. McDonald, I.K., and Thornton, J.M. (1994). Satisfying hydrogen bonding potential in proteins. J. Mol. Biol. 238, 777-793.
48. McRee, D.E. (1993). Practical Protein Crystallography (San Diego: Academic Press).
49. Minor, W. (1993). XDISPLAYF program (West Lafayette: Purdue University).
50. Nicholls, A., Sharp, K.A., and Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
51. Oldstone, M.B. (1987). Molecular mimicry and autoimmune disease. Cell 50, 819-820.
52. Otwinowski, Z. (1993). Oscillation data reduction program. In Proceedings of the CCP4 Study Weekend, L. Sawyer, N. Isaacs, and S. Bailey, eds. (Daresbury, UK: SERC Daresbury Laboratory), pp. 56-62.
53. bm3. J. Immunol. 143, 1674-1679.
54. Rammensee, H.G., Friede, T., and Stevanoviic, S. (1995). MHC ligands and peptide motifs: first listing, Immunogenetics 41, 178-228.
55. Read, R.J. (1986). Improved fourier coefficients for maps using phases from partial structures with errors. Acta Cryst. A42, 140-149.
56. Rice, L.M., and Brünger, AT. (1994). Torsion angle dynamics: reduced variable conformational sampling enhances crystallographic structure refinement. Proteins 19, 277-290.
57. Saper, M.A., Bjorkman, P.J., and Wiley, D.C. (1991). Refined structure of the human histocompatibility antigen HLA-A2at 2.6 Å resolution. J. Mol. Biol. 219, 277-319.
58. d and the T cell receptor. J. Immunol. 157, 4478-4485.
59. Schlueter, C.J., Schodin, B.A., Tetin, S.Y., and Kranz, D.M. (1996b). Specificity and binding properties of a single-chain T cell receptor. J. Mol. Biol. 256, 859-869.
60. Schreiber, G., Frisch, C., and Fersht, A.R. (1997). The role of Glu73 of barnase in catalysis and the binding of barstar. J. Mol. Biol. 270, 111-122.
61. Sha, W.C., Nelson, C.A., Newberry, R.D., Kranz, D.M., Russell, J.H., and Loh, D.Y. (1988). Positive and negative selection of an antigen receptor on T cells intransgenic mice. Nature 336, 73-76.
62. b antigen is altered by Kb mutations that involve peptide binding. Proc. Natl. Acad. Sci. USA 87, 6186-6190.
63. Sheriff, S., Hendrickson, W.A., and Smith, J.L. (1987). Structure of myohemerythrin in the azidomet state at 1.7/1.3 Å resolution. J. Mol. Biol. 197, 273-296.
64. Sherman, L.A., and Chattopadhyay, S. (1993). The molecular basis of allorecognition. Annu. Rev. Immunol. 11, 385-402.
65. Smith, T.J. (1995). MolView: a program for analyzing and displaying atomic structures on the Macintosh personal computer. J. Mol. Graph. 13, 122-125.
66. Sykulev, Y., Brunmark, A., Jackson, M., Cohen, R.J., Peterson, P.A., and Eisen, H.N. (1994a). Kinetics and affinity of reactions between an antigen-specific T cell receptor and peptide-MHC complexes. Immunity 1, 15-22.
67. Sykulev, Y., Brunmark, A., Tsomides, T.J., Kageyama, S., Jackson, M., Peterson, P.A., and Eisen, H.N. (1994b). High-affinity reactions between antigen-specific T-cell receptors and peptides associated with allogeneic and syngeneic major histocompatibility complex class I proteins. Proc. Natl. Acad. Sci. USA 91, 11487-11491.
68. bm3 molecule. J. Immunol. 155, 2419-2426.
69. Tallquist, M., Yun, T., and Pease, L. (1996). A single T cell receptor recognizes structurally distinct MHC/peptide complexes with high specificity. J. Exp. Med. 184, 1017-1026.
70. Tallquist, M.D., Weaver, A.J., and Pease, L.R. (1998). Degenerative recognition of alloantigenic peptides on a positively-selecting class I molecule. J. Immunol. 160, 802-809.
71. d complex. Mol. Immunol. 31, 705-711.
72. Townsend, A.R., Rothbard, J., Gotch, P.M., Bahadur, G., Wraith, D., and McMichael, A.J. (1986). Theepitopes of influenza nucleoprotein recognized by cytotoxic T lymphocytes can be defined with short synthetic peptides. Cell 44, 959-968.
73. Udaka, K., Tsomides, T.J., Walden, P., Fukusen, N., and Eisen, H.N. (1993). A ubiquitous protein is the source of naturally occurring peptides that are recognized by a CD8 T-cell clone. Proc. Natl. Acad. Sci. USA 90, 11272-11276.
74. Udaka, K., Wiesmuller, K.H., Kienle, S., Jung, G., and Walden, P. (1996). Self-MHC-restricted peptides recognized by an alloreactive T lymphocyte clone. J. Immunol. 157, 670-678.
75. Vellieux, F.M.D. (1993). DEMON program suite (Grenoble, France).
76. Wukovitz, S.W., and Yeates, T.O. (1995). Why protein crystals favour some space-groups over others. Nat. Struct. Biol. 2, 1062-1067.
77. d at 2.4 Å resolution: implications for antigen-determinant selection. Cell 76, 39-50.
78. Zinkernagel, R.M., and Doherty, P.C. (1974). Restriction of in vitro T cell-mediated cytotoxicity in lymphocytic choriomeningitis within a syngeneic or semiallogeneic system. Nature 248, 701-702.