Crystal structures of HLA-A*0201 complexed with antigenic peptides with either the amino- or carboxyl-terminal group substituted by a methyl group

Proteins: Structure, Function and Genetics

Volumn 33, Issue 1, 1998, Pages 97-106

  Bouvier, Marlène ^a,c   Guo, Hwai Chen ^a,d   Smith, Kathrine J ^b   Wiley, Don C ^a,b  

^a HARVARD UNIVERSITY   (United States)

^b BOSTON CHILDREN S HOSPITAL   (United States)

^c UNIVERSITY OF CONNECTICUT   (United States)

^d BOSTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Antigenic peptides; Class I MHC molecules; HLA A2 complexes; Hydrogen bonds; Protein structure

Indexed keywords

HLA A ANTIGEN;

AMINO ACID SEQUENCE; ARTICLE; CRYSTAL STRUCTURE; HUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS;

CRYSTALLOGRAPHY, X-RAY; HLA-A2 ANTIGEN; HUMANS; INFLUENZA A VIRUS; PEPTIDES; PROTEIN CONFORMATION; VIRAL MATRIX PROTEINS;

EID: 0032189076     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19981001)33:1<97::AID-PROT9>3.0.CO;2-I     Document Type: Article

References (33)

1. Falk, K., Rötzschke, O., Stevanovic, S., Jung, G. and Rammensee, H.-G. Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules. Nature 351:290-296, 1991.
2. Townsend, A. and Bodmer, H. Antigen recognition by class I-restricted T lymphocytes. Ann. Rev. Immunol. 7:601-624, 1989.
3. Stern, L.J. and Wiley, D.C. Antigenic peptide binding by class I and class II histocompatibility proteins. Structure 2:245-251, 1994.
4. Madden, D.R. The three-dimensional structure of peptide-MHC complexes. Ann. Rev. Immunol. 13:587-622, 1995.
5. Garboczi, D.N., Ghosh, P., Utz, U., Fan, Q.R., Biddison, W.E. and Wiley, D.C. Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. Nature 384:134-141, 1996.
6. Guo, H.-C., Madden, D.R., Silver, M.L. et al. Comparison of the P2 specificity pocket in three human histocompatibility antigens: HLA-A*6801, HLA-A*0201, and HLA-B*2705. Proc. Natl. Acad. Sci. USA 90:8053-8057, 1993.
7. Ruppert, J., Sidney, J., Celis, E., Kubo, R.T., Grey, H.M. and Sette, A. Prominent role of secondary anchor residues in peptide binding to HLA-A2.1 molecules. Cell 74:929-937, 1993.
8. Saito, Y., Peterson, P.A. and Matsumura, M. Quantitation of peptide anchor residue contributions to class I major histocompatibility complex molecule binding. J. Biol. Chem. 268:21309-21317, 1993.
9. Bouvier, M. and Wiley, D.C. Importance of antigenic peptide amino and carboxyl termini to the stability of class I MHC molecules. Science 265:398-402, 1994.
10. Bednarek, M.A., Sauma, S.Y., Gammon, M.C. et al. The minimum peptide epitope from the influenza virus matrix protein. Extra and intracellular loading of HLA-A2. J. Immunol. 147:4047-4053, 1991.
11. Holm, R.H., Chakravatory, A., Dudek, G.O. A nuclear resonance study of conformational equilibria. J. Am. Chem. Soc. 86:379-387, 1964.
12. Garboczi, D.N., Hung, D.T. and Wiley, D.C. HLA-A2-peptide complexes: Refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peptides. Proc. Natl. Acad. Sci. USA 89: 3429-3433, 1992.
13. Garboczi, D.N., Madden, D.R. and Wiley, D.C. Five viral peptide-HLA-A2 co-crystals. Simultaneous space group determination and X-ray data collection. J. Mol. Biol. 239:581-587, 1994.
14. Kabsch, W. Evaluation of single crystal X-ray diffraction data from a position-sensitive detector. J. Appl. Crystallogr. 21:916-924, 1988.
15. Navaza, J. On the fast rotation function. Acta Crystallogr. A43:645-653, 1987.
16. Brünger, A.T. Crystallographic refinement by simulated annealing Application to a 2.8Å resolution structure of aspartate aminotransferase. J. Mol. Biol. 203:803-816, 1988.
17. Guo, H.-C., Jardetzky, T.S., Garrett, T.P.J., Lane, W.S., Strominger, J.L. and Wiley, D.C. Different length peptides bind to HLA-Aw68 similarly at their ends but bulge out in the middle. Nature 360:364-366, 1992.
18. Madden, D.R., Garboczi, D.N. and Wiley, D.C. The antigenic identity of peptide-MHC complexes: A comparison of the conformations of five viral peptides presented by HLA-A2. Cell 75:693-708, 1993.
19. Brünger, A.T. Free R value: A novel statistical quantity for assessing the accuracy of crystal structures. Nature 355:472-475, 1992.
20. Brünger, A.T., Krukowski, A. and Erickson, J. Slow-cooling protocols for crystallographic refinement by simulated annealing. Acta Crystallogr. A46:585-593, 1990.
21. Madden, D.R., Gorga, J.C., Strominger, J.L. and Wiley, D.C. The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation. Nature 353: 321-325, 1991.
22. b. Science 257:919-927, 1992.
23. Matsumura, M., Fremont, D.H., Peterson, P.A. and Wilson, I.A. Emerging principles for the recognition of peptide antigens by MHC class I molecules. Science 257:927-934, 1992.
24. b molecule containing a single viral peptide: Implications for peptide binding and T cell receptor recognitions. Proc. Natl. Acad. Sci. 89:8403-8407, 1992.
25. Silver, M.L., Guo, H.-C., Strominger, J.L. and Wiley, D.C. Atomic structure of a human MHC molecule presenting an influenza virus peptide. Nature 360:367-369, 1992.
26. Collins, E.J., Garboczi, D.N. and Wiley, D.C. Three-dimensional structure of a peptide extending from one end of a class I MHC binding site. Nature 371:626-629, 1994.
27. Smith, K.J., Reid, S.W., Stuart, D.I., McMichael, A.J., Jones, E.Y., Bell, J.I. An altered position of the α2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501. Immunity 4:203-213, 1996.
28. Smith, K.J., Reid, S.W., Harlos, K. et al. Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53. Immunity 4:215-228, 1996.
29. Madden, D.R., Gorga, J.C., Strominger, J.L., Wiley, D.C. The three-dimensional structure of HLA-B27 at 2.1Å resolution suggests a general mechanism for tight peptide binding to MHC. Cell 70:1035-1048, 1992.
30. Becktel, W.J. and Schellman, J.A. Protein stability curves. Biopolymers 26:1859-1877, 1987.
31. Latron, F., Pazmany, L., Morrison, J. et al. A critical role for conserved residues in the cleft of HLA-A2 in presentation of a nonapeptide to T cells. Science 257:964-967, 1992.
32. Dessen, A., Lawrence, C.M., Cupo, S., Zaller, D.M. and Wiley, D.C. X-ray crystal structure of HLA-DR4 (DRA1*0101, DRB1*0401) complexed with a peptide from human collagen II. Immunity 7:473-481, 1997.
33. Laskowski, R.A., MacArthur, M.W., Moss, D.S. and Thornton, J.M. PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26:28-29, 1993.