MHC class I and class II structures

Current Opinion in Immunology

Volumn 9, Issue 1, 1997, Pages 75-79

  Jones, E Yvonne ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2;

AMINO ACID SEQUENCE; ARTICLE; CRYSTAL STRUCTURE; HUMAN; HYDROGEN BOND; MAJOR HISTOCOMPATIBILITY COMPLEX; MOUSE; NONHUMAN; PROTEIN SECONDARY STRUCTURE;

EID: 0031051784     PISSN: 09527915     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0952-7915(97)80162-8     Document Type: Article

References (39)

1. Bjorkman PJ, Saper MA, Samraoui B, Bennett WS, Strominger JL, Wiley DC. Structure of the human class I histocompatibility antigen HLA-A2. Nature. 329:1987;506-512.
2. Brown JH, Jardetzky TS, Gorga JC, Stern LJ, Urban RG, Strominger JL, Wiley DC. Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1. Nature. 364:1993;33-39.
3. Madden DR. The three-dimensional structure of peptide-MHC complexes. of special interest Annu Rev Immunol. 13:1995;587-622 A clear and comprehensive review of the information available up to 1995.
4. Garrett TPJ, Saper MA, Bjorkman PJ, Strominger JL, Wiley DC. Specificity pockets for the side chains of peptide antigens in HLA-Aw68. Nature. 342:1989;692-696.
5. Saper MA, Bjorkman PJ, Wiley DC. Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution. J Mol Biol. 219:1991;277-319.
6. Madden DR, Gorga JC, Strominger JL, Wiley DC. The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation. Nature. 353:1991;321-325.
7. Guo H-C, Jardetzky TS, Garrett TPJ, Lane WS, Strominger JL, Wiley DC. Different length peptides bind to HLA-Aw68 similarly at their ends but bulge out in the middle. Nature. 360:1992;364-366.
8. Madden DR, Gorga JC, Strominger JL, Wiley DC. The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC. Cell. 70:1992;1035-1048.
9. *2705. Proc Natl Acad Sci USA. 90:1993;8053-8057.
10. Garboczi DN, Hung DT, Wiley DC. HLA-A2-peptide complexes: refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peptides. Proc Natl Acad Sci USA. 89:1992;3429-3433.
11. Stura EA, Matsumura M, Fremont DH, Saito Y, Peterson PA, Wilson IA. Crystallization of murine major histocompatibility complex class I H-2Kb with single peptides. J Mol Biol. 228:1992;975-982.
12. Fremont DH, Matsumura M, Stura EA, Peterson PA, Wilson IA. Crystal structures of two viral peptides in complex with murine MHC class I H-2Kb. Science. 257:1992;919-927.
13. Matsumura M, Fremont DH, Peterson PA, Wilson IA. Emerging principles for the recognition of peptide antigens by MHC class I molecules. Science. 257:1992;927-934.
14. Zhang W, Young ACM, Imarai M, Nathenson SG, Sacchettini JC. Crystal structure of the major histocompatibility complex class I H-2Kb molecule containing a single viral peptide: implications for peptide binding and T-cell receptor recognition. Proc Natl Acad Sci USA. 89:1992;8403-8407.
15. Young ACM, Zhang W, Sachettini JC, Nathenson SG. The three-dimensional structure of H-2Db at 2.4 Å resolution: implications for antigen-determinant selection. Cell. 76:1994;39-50.
16. Madden DR, Garboczi DN, Wiley DC. The antigenic identity of peptide-MHC complexes: a comparison of the conformations of five viral peptides presented by HLA-A2. Cell. 75:1993;693-708.
17. Silver ML, Guo H-C, Strominger JL, Wiley DC. Atomic structure of a human MHC molecule presenting an influenza virus peptide. Nature. 360:1992;367-369.
18. Reid SW, Smith KJ, Jakobsen BK, O'Callaghan CA, Reyburn H, Harlos K, Stuart DI, McMichael AJ, Bell JI, Jones EY. Production and crystallization of MHC class I B allele single peptide complexes. of special interest FEBS Lett. 383:1996;119-123 Methodology for expression and crystallization of HLA-B allele single peptide complexes.
19. Wang C-R, Castano AR, Peterson PA, Slaughter C, Lindahl KF, Deisenhofer J. Nonclassical binding of formylated peptide in crystal structure of the MHC class Ib molecule H2-M3. Cell. 82:1995;655-664 The first structure for this murine MHC class Ib molecule. H2-M3 has an unusual preference for binding amino-formylated peptides. The structure reveals that for such peptides the P1 sidechain occupies the B pocket, a position normally taken by the P2 sidechain, thus allowing H2-M3 to make specific alterations at the A pocket end of the binding groove to accommodate the formyl group.
20. Smith KJ, Reid SW, Harlos K, McMichael AJ, Stuart DI, Bell JI, Jones EY. Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53. of outstanding interest Immunity. 4:1996;215-228 The first structural information on the human allele HLA-B53. Comparison of two specific peptide HLA-B53 complexes provides striking examples of the role of bound water molecules in essential fine tuning of the fit between MHC and peptide.
21. *3501. The complex with an 8-mer peptide unexpectedly reveals a nonstandard positioning of the peptide amino-terminus and a significant shift in the amino-terminal portion of the α2 helix which correlates with the position of the peptide carboxy-terminus.
22. Weiss GA, Collins EJ, Garboczi DN, Wiley DC, Schreiber SL. A tricyclic ring-system replaces the variable regions of peptides presented by 3 alleles of human MHC class-I molecules. of outstanding interest Chem Biol. 2:1995;401-407 A nice example of structure guided design showing that it is possible to use a generic, organic linker (specifically the aromatic compound phenanthridine) to replace the central portion of class I presented peptides. Ultimately such nonpeptidic MHC ligands may be of therapeutic use.
23. Bouvier M, Wiley DC. Antigenic peptides containing large PEG loops designed to extend out of the HLA-A2 binding-site form stable complexes with class-I major histocompatibility complex-molecules. Proc Natl Acad Sci USA. 93:1996;4583-4588 Another exotic peptide designed on the basis of the established structural information for physiological peptide HLA-A2 complexes. In this example the aim is to produce compounds which sterically hinder recognition by TCRs.
24. Collins EJ, Garboczi DN, Karpusas MN, Wiley DC. The three-dimensional structure of a class I major histocompatibility complex molecule missing the α3 domain of the heavy chain. of outstanding interest Proc Natl Acad Sci USA. 92:1995;1218-1221 A fortuitous demonstration that the α3 domain does not influence the conformation of the peptide binding groove, at least not once the groove is occupied by peptide.
25. b. This paper also contains a good example of a bound water molecule optimizing the fit between peptide and MHC.
26. Bouvier M, Wiley DC. Importance of peptide amino and carboxyl termini to the stability of MHC class-I molecules. Science. 265:1994;398-402.
27. Collins EJ, Garboczi DN, Wiley DC. Three-dimensional structure of a peptide extending from one end of a class I MHC binding site. Nature. 371:1994;626-629.
28. Brown JH, Jardetzky TS, Stern LJ, Gorga JC, Strominger JL, Wiley DC. Human class-II MHC molecule HLA-DR1-X-ray structure determined from 3 crystal forms. of special interest Acta Cryst D. 51:1995;946-961 An impressive account of the methodological firepower brought to bear in the first structure determination of an MHC class II molecule.
29. Stern LJ, Brown JH, Jardetzky TS, Gorga JC, Urban RG, Strominger JL, Wiley DC. Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide. Nature. 368:1994;215-221.
30. Fremont DH, Hendrickson WA, Marrack P, Kappler J. Structures of an MHC class II molecule with covalently bound single peptides. of outstanding interest Science. 272:1996;1001-1004 The first structures for a murine MHC class II molecule. The structures illustrate the efficacy, for specific complex production, of covalently tethering the peptide of interest to the MHC β chain. Comparison with the human MHC class II structures highlights the role of certain MHC residues in influencing peptide binding in a potentially pH-dependant manner.
31. Ghosh P, Amaya M, Mellins E, Wiley DC. The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3. of outstanding interest Nature. 378:1995;457-462 A view of a key stage in the mechanism of MHC class II maturation. The complex also provides a structure for a second human MHC class II molecule.
32. Jardetzky TS, Brown JH, Gorga JC, Stern LJ, Urban RG, Strominger JL, Wiley DC. Crystallographic analysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline II-like conformation for bound peptides. of outstanding interest Proc Natl Acad Sci USA. 93:1996;734-738 Good quality electron density for the region of the peptide mix which lies within the MHC class II peptide binding groove indicates that the same mainchain conformation is imposed on all bound peptides.
33. Cresswell P. Invariant chain structure and MHC class II function. of special interest Cell. 84:1996;505-507 A timely review of the state of play for structure-based models of MHC class II maturation.
34. Jasanoff A, Park SJ, Wiley DC. Direct observation of disordered regions in the major histocompatibility complex class II-associated invariant chain. of special interest Proc Natl Acad Sci USA. 92:1995;9900-9904 An account of the efficacious use of nuclear magnetic resonance methods to demonstrate the presence of discrete, disordered regions in the Ii.
35. Park SJ, Sadeghnasseri S, Wiley DC. Invariant chain made in Escherichia coli has an exposed amino-terminal segment that blocks antigen-binding to HLA-DR1 and a trimeric carboxy-terminal segment that binds empty HLA-DR1. of special interest Proc Natl Acad Sci USA. 92:1995;11289-11293 Careful dissection of the differing functional roles of regions of the Ii in interaction with MHC class II molecules.
36. Burmeister WP, Gastinel LN, Simister NE, Blum ML, Bjorkman PJ. Crystal-structure at 2.2 Å resolution of the MHC-related neonatal Fc receptor. Nature. 372:1994;336-343.
37. Wilson IA. Another twist to MHC-peptide recognition. of special interest Science. 272:1996;973-974 Succinct summary of the state of play in our understanding of the basic structure/function principles for MHC molecules.
38. Jardetzky TS, Brown JH, Gorga JC, Stern LJ, Urban RG, Chi YI, Stauffacher C, Strominger JL, Wiley DC. 3-dimensional structure of a human class-II histocompatibility molecule complexed with superantigen. Nature. 368:1994;711-718.
39. Kim JS, Urban RG, Strominger JL, Wiley DC. Toxin shock syndrome toxin-1 complexed with a class-II major histocompatibility molecule HLA-DR1. Science. 266:1994;1870-1874.