Crystal structure of I-A(k) in complex with a dominant epitope of lysozyme

Immunity

Volumn 8, Issue 3, 1998, Pages 305-317

  Fremont, Daved H ^a,b   Monnaie, Didier ^b   Nelson, Christopher A ^b   Hendrickson, Wayne A ^a   Unanue, Emil R ^b  

^a Och Spine at New York Presbyterian Hospitals   (United States)

^b WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; LYSOZYME; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; PEPTIDE; T LYMPHOCYTE RECEPTOR;

ANIMAL CELL; ANTIGEN PRESENTATION; ARTICLE; BINDING AFFINITY; CHO CELL; COMPLEX FORMATION; CRYSTAL STRUCTURE; MAJOR HISTOCOMPATIBILITY COMPLEX; NONHUMAN; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; T LYMPHOCYTE ACTIVATION;

EID: 0032033445     PISSN: 10747613     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-7613(00)80536-1     Document Type: Article

References (50)

1. Acha-Orbea, H., and McDevitt, H.O. (1987). The first external domain of the non-obese diabetic mouse class II I-A beta chain is unique. Proc. Natl. Acad. Sci USA 84, 2435-2442.
2. Adorini, L., Appella, E., Doria, G., and Nagy, Z.A. (1988). Mechanisms influencing the immunodominance of T cell determinants. J. Exp. Med. 168, 2091-2104.
3. Allen, P.M., and Unanue, E.R. (1984). Differential requirements for antigen processing by macrophages for lysozyme-specific T cell hybridomas. J. Immunol. 132, 1077-1079.
4. Allen, P.M., Matsueda, G.R., Evans, R.J., Dunbar, J.B. Jr., Marshall, G.R., and Unanue, E.R. (1987). Identification of the T-cell and Ia contact residues of a T-cell antigenic epitope. Nature 327, 713-715.
5. Babbitt, B.P., Allen, P.M., Matsueda, G., Haber, E., and Unanue, E.R. (1985). Binding of immunogenic peptides to Ia histocompatibility molecules. Nature 317, 359-361.
6. Brown, J.H., Jardetzky, T.S., Gorga, J.C., Stern, L.J., Urban, R.G., Strominger, J.L., and Wiley, D.C. (1993). Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1. Nature 364, 33-39.
7. Buus, S., Sette, A., Colon, S.M., Miles, C., and Grey, H.M. (1987). The relation between major histocompatibility complex (MHC) restriction and the capacity of Ia to bind immunogenic peptides. Science 235, 1353-1358.
8. Brunger, A.T, Kuriyan, J., and Karplus, M. (1987). Crystallographic R-factor refinement by molecular dynamics. Science 235, 458-460.
9. Carson, M. (1987). Ribbon models of macromolecules. J. Mol. Graphics 5, 103-106.
10. Carson, R.T., Vignali, K.M., Woodland, D.L., and Vignali, D.A. (1997). T cell receptor recognition of MHC class II-bound peptide flanking residues enhances immunogenicity and results in altered TcR V region usage. Immunity 7, 387-400.
11. Connolly, M.L. (1993). The molecular surface package. J. Mol. Graphics 11, 139-141.
12. Cosgrove, D., Bodmer, H., Bogue, M., Benoist, C., and Mathis, D. (1992). Evaluation of the functional equivalence of major histocompatible complex class II A and E complexes. J. Exp. Med. 176, 629-634.
13. Dadaglio, G., Nelson, C.A., Deck, M.B., Petzold, S.J., and Unanue, E.R. (1997). Characterization and quantitation of peptide-MHC complexes produced from hen egg lysozyme using a monoclonal antibody. Immunity 6, 727-738.
14. Derewenda, Z.S., Derewenda, U., and Kobos P.M. (1994). (His)C epsilon-H...O=C < hydrogen bond in the active sitesof serine hydrolases. J. Mol. Biol. 241, 83-93.
15. Dessen, A., Lawrence, C.M., Cupo, S., Zaller, D.M., and Wiley, D.C. (1997). X-ray crystal structure of HLA-DR4 (DRA*0101, DRB1*0401) complexed with a peptide from human collagen II. Immunity 7 473-481.
16. Figueroa, F., Tichy H., Singleton, G., Franquedakis-Tsolis, S., and Klein, J. (1989). High frequency of H-2-E0 alleles among wild mice. Immunogenetics 30, 222-225.
17. Figueroa, F., Gutknecht, J., Tichy H., and Klein, J. (1990). Class II MHC genes in rodent evolution. Immunol. Rev. 113, 27-46.
18. b. Science 257, 919-927.
19. Fremont, D.H., Hendrickson, W.A., Marrack, P., and Kappler, J.W. (1996). Structures of an MHC class II molecule with covalently bound single peptides. Science 272, 1001-1004.
20. 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.
21. 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.
22. Ghosh, P., Amaya, M., Mellins, E., and Wiley, D.C. (1995). The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3. Nature 378, 457-462.
23. Harding, C.V., Roof, R.W., Allen, P.M., and Unanue E.R. (1991). Effects of pH and polysaccharides on peptide binding to class II major histocompatibility complex molecules. Proc. Natl. Acad. Sci. USA 88, 2740-2744.
24. Heinz, D.W., Baase, W.A., Dahlquist, F.W., and Matthews, B.W. (1993). How amino-acid insertions are allowed in an alpha-helix of T4 lysozyme. Nature 361, 561-564.
25. Jardetzky, T.S., Brown, J.H., Gorga, J.C., Stern, L.J., Urban, R.G., Strominger, J.L., and Wiley, D.C. (1996). Crystallographic analysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline II-like conformation for bound peptides. Proc. Natl. Acad. Sci. USA 93, 734-738.
26. Jones, T.A. (1978). A graphical model building and refinement system for macromolecules. J. Appl. Crystallogr. 11, 268-272.
27. Jones, T.A., Zou, J.Y., Cowan, S.W., and Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta. Crystallogr. A 47, 110-119.
28. Kabat, E.A., Wu, T.T., Perry, H.M., Gottesman, K.S., and Foeller, C. (1991). Sequences of Proteins of Immunological Interest, Fifth Edition (Bethesda, MD: National Institutes of Health, National Center for Biotechnology Information), NIH publication no. 91-3242, p. 2597.
29. Kabsch, W., and Sander, C. (1983). Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637.
30. Kozono, H., White, J., Clements, J., Marrack, P., and Kappler, J.W. (1994). Functional soluble major histocompatibility complex proteins with covalently bound peptides. Nature 369, 151-154.
31. Low, M.G. (1992). Phospholipases that degrade the glycosyl-phosphatidyl inositol anchor of membrane proteins. In Lipid Modification of Proteins: A Practical Approach, N.M. Hooper and A.J. Turner, eds. (New York: Oxford University Press), pp. 117-154.
32. Marrack, P., Ignatowicz, L., Kappler, J.W., Boymel, J., and Freed, J.H. (1993). Comparison of peptides bound to spleen and thymus class II. J. Exp. Med. 178, 2173-2183.
33. k. Proc. Natl. Acad. Sci. USA 89, 7380-7383.
34. k. J. Immunol. 157, 755-762.
35. k α-chain required for the binding and stability of two antigenic peptides. J. Immunol. 156, 176-182.
36. k. Immunol. Rev. 151, 81-105.
37. Nizetic, D., Figueroa, F., Dembic, Z., Nevo, E., and Klein, J. (1987). Major histocompatibility complex gene organization in the mole rat, Spalax ehrenbergi: evidence for transfer of function between class II genes. Proc. Natl. Acad. Sci. USA 84, 5828-5832.
38. Otwinowski, Z. (1993). Oscillation data reduction program. In Proceedings of the CCP4 Study Weekend: Data Collection and Processing, 29-30 January, 1993, L. Sawyer, N. Isaacs, and S. Bailey, compilers (Warrington, England: SERC Daresbury Laboratory), pp. 56-62.
39. Reay, P.A., Wettstein, D.A., and Davis, M.M. (1992). pH dependence and exchange of high and low responder peptides binding to a class II MHC molecule. EMBO J. 11, 2829-2839.
40. Reay, P.A., Kantor, R.M., and Davis M.M. (1994). Use of global amino acid replacements to define the requirements for MHC binding and T-cell recognition of moth cytochrome c (93-103). J. Immunol. 152, 3946-3957.
41. Richardson, J.S., Getzoff, E.D., and Richardson, D.C. (1978). The beta bulge: a common small unit of nonrepetitive protein structure. Proc. Natl. Acad. Sci. USA 75, 2574-2578.
42. Rudensky, A.Y., Preston-Hurlburt, P., Hong, S.C., Barlow, A., and Janeway, C.A. Jr. (1991). Sequence analysis of peptides bound to MHC class II molecules. Nature 353, 622-627.
43. Sant, A.J., Braunstein, N.S., and Germain, R.N. (1987). Predominant role of amino-terminal sequences in dictating efficiency of class II major histocompatibility complex alpha beta dimer expression. Proc. Natl. Acad. Sci. USA 84, 8065-8069.
44. Sant'Angelo, D.B., Waterbury, G., Preston-Hurlburt, P., Yoon, S.T., Medzhitov, R., Hong, S.C., and Janeway, C.A. Jr. (1996). The specificity and orientation of a TCR to its peptide-MHC class II ligands. Immunity 4, 367-376.
45. Smith, K.J., Reid, S.W., Stuart, D.I., McMichael, A.J., Jones, E.Y., and Bell, J.I. (1996). An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501. Immunity 4, 203-213.
46. Spencer, J.S., Freed, J.H., and Kubo, R.T. (1993). Expression and function of mixed isotype MHC class II molecules in normal mice. J. Immunol. 151, 6822-6832.
47. Stern, L., Brown, G., Jardetzky, T., Gorga, J., Urban, R., Strominger, J., and Wiley, D. (1994). Crystal structure of the human class II MHC protein HLA-DR1 complexed with an antigenic peptide from influenza virus. Nature 368, 215-221.
48. Todd, J.A., Bell, J.I., and McDevitt, H.O. (1987). HLA-DQ beta gene contributes to susceptibility and resistance to insulin-dependent diabetes mellitus. Nature 329,599-602.
49. Viner, N.J., Nelson, C.A., Deck, B., and Unanue, E.R. (1996). Complexes generated by the binding of free peptides to class II MHC molecules are antigenically diverse compared with those generated by intracellular processing. J. Immunol. 156, 2365-2368.
50. Wettstein, D.A., Boniface, J.J., Reay, P.A., Schild, H., and Davis, M.M. (1991). Expression of a class II major histocompatibility complex (MHC) heterodimer in a lipid-linked form with enhanced peptide/soluble MHC complex formation at low pH. J. Exp. Med. 174, 219-228.