Structural and functional mosaic nature of MHC class I molecules in their peptide-free form

Molecular Immunology

Volumn 55, Issue 3-4, 2013, Pages 393-399

  Kurimoto, Eiji ^a,b   Kuroki, Kimiko ^c   Yamaguchi, Yoshiki ^a,d   Yagi Utsumi, Maho ^a,e   Igaki, Takahiro ^a   Iguchi, Takeshi ^f   Maenaka, Katsumi ^c,g   Kato, Koichi ^a,e  

^a NAGOYA CITY UNIVERSITY   (Japan)

^b MEIJO UNIVERSITY   (Japan)

^c HOKKAIDO UNIVERSITY   (Japan)

^d RIKEN   (Japan)

^e INSTITUTE FOR MOLECULAR SCIENCE   (Japan)

^f Fujiya Co Ltd   (Japan)

^g JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

2 microglobulin; MHC class I; NK cell receptors; NMR; Peptide free form; Refolding

Indexed keywords

MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1;

ANTIGEN STRUCTURE; ARTICLE; CONTROLLED STUDY; ESCHERICHIA COLI; IN VITRO STUDY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION;

BETA 2-MICROGLOBULIN; ENDOPLASMIC RETICULUM; HISTOCOMPATIBILITY ANTIGENS CLASS I; HLA-C ANTIGENS; HUMANS; KILLER CELLS, NATURAL; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROTEIN FOLDING; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84877588713     PISSN: 01615890     EISSN: 18729142     Source Type: Journal    
DOI: 10.1016/j.molimm.2013.03.014     Document Type: Article

References (37)

1. Arnold K., Bordoli L., Kopp J., Schwede T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 2006, 22:195-201.
2. Arosa F.A., Santos S.G., Powis S.J. Open conformers: the hidden face of MHC-I molecules. Trends in Immunology 2007, 28:115-123.
3. b by the NK cell inhibitory receptor Ly49C. Journal of Immunology 2005, 175:3542-3553.
4. Bjorkman P.J., Saper M.A., Samraoui B., Bennett W.S., Strominger J.L., Wiley D.C. Structure of the human class I histocompatibility antigen, HLA-A2. Nature 1987, 329:506-512.
5. 2m heterodimer. Nature Structural Biology 1998, 5:377-384.
6. Boyington J.C., Motyka S.A., Schuck P., Brooks A.G., Sun P.D. Crystal structure of an NK cell immunoglobulin-like receptor in complex with its class I MHC ligand. Nature 2000, 405:537-543.
7. Elliott T., Cerundolo V., Elvin J., Townsend A. Peptide-induced conformational change of the class I heavy chain. Nature 1991, 351:402-406.
8. Fahnestock M.L., Tamir I., Narhi L., Bjorkman P.J. Thermal stability comparison of purified empty and peptide-filled forms of a class I MHC molecule. Science 1992, 258:1658-1662.
9. Falk K., Rotzschke O., Grahovac B., Schendel D., Stevanovic S., Gnau V., Jung G., Strominger J.L., Rammensee H.G. Allele-specific peptide ligand motifs of HLA-C molecules. Proceedings of the National Academy of Sciences of the United States of America 1993, 90:12005-12009.
10. Fan Q.R., Long E.O., Wiley D.C. Crystal structure of the human natural killer cell inhibitory receptor KIR2DL1-HLA-Cw4 complex. Nature Immunology 2001, 2:452-460.
11. Guex N., Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 1997, 18:2714-2723.
12. Hansen T.H., Lybarger L., Yu L., Mitaksov V., Fremont D.H. Recognition of open conformers of classical MHC by chaperones and monoclonal antibodies. Immunological Reviews 2005, 207:100-111.
13. 2-microglobulin and the evolution of interfaces in MHC class I molecules. Immunogenetics 2013, 65:157-172.
14. Kainosho M., Tsuji T. Assignment of the three methionyl carbonyl carbon resonances in streptomyces subtilisin inhibitor by a carbon-13 and nitrogen-15 double-labeling technique. A new strategy for structural studies of proteins in solution. Biochemistry 1982, 21:6273-6279.
15. Lebrón J.A., Bennett M.J., Vaughn D.E., Chirino A.J., Snow P.M., Mintier G.A., Feder J.N., Bjorkman P.J. Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor. Cell 1998, 93:111-123.
16. Ljunggren H.G., Stam N.J., Ohlén C., Neefjes J.J., Höglund P., Heemels M.T., Bastin J., Schumacher T.N., Townsend A., Kärre K., et al. Empty MHC class I molecules come out in the cold. Nature 1990, 346:476-480.
17. Madden D.R., Gorga J.C., Strominger J.L., Wiley D.C. The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation. Nature 1991, 353:321-325.
18. Mage M.G., Dolan M.A., Wang R., Boyd L.F., Revilleza M.J., Robinson H., Natarajan K., Myers N.B., Hansen T.H., Margulies D.H. The peptide-receptive transition state of MHC class I molecules: insight from structure and molecular dynamics. Journal of Immunology 2012, 189:1391-1399.
19. 13C NMR spectroscopy. Journal of Biochemistry 2006, 140:591-598.
20. Olson R., Huey-Tubman K.E., Dulac C., Bjorkman P.J. Structure of a pheromone receptor-associated MHC molecule with an open and empty groove. PLoS Biology 2005, 3:e257.
21. Ortiz-Navarrete V., Hämmerling G.J. Surface appearance and instability of empty H-2 class I molecules under physiological conditions. Proceedings of the National Academy of Sciences of the United States of America 1991, 88:3594-3597.
22. Paulsson K., Wang P. Chaperones and folding of MHC class I molecules in the endoplasmic reticulum. Biochimica et Biophysica Acta 2003, 1641:1-12.
23. Pervushin K., Riek R., Wider G., Wüthrich K. Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proceedings of the National Academy of Sciences of the United States of America 1997, 94:12366-12371.
24. Rudolph M.G., Stanfield R.L., Wilson I.A. How TCRs bind MHCs, peptides, and coreceptors. Annual Review of Immunology 2006, 24:419-466.
25. Saunders P.M., van Endert P. Running the gauntlet: from peptide generation to antigen presentation by MHC class I. Tissue Antigens 2011, 78:161-170.
26. Schulman B.A., Kim P.S., Dobson C.M., Redfield C. A residue-specific NMR view of the non-cooperative unfolding of a molten globule. Nature Structural Biology 1997, 4:630-634.
27. Schumacher T.N., Heemels M.T., Neefjes J.J., Kast W.M., Melief C.J., Ploegh H.L. Direct binding of peptide to empty MHC class I molecules on intact cells and in vitro. Cell 1990, 62:563-567.
28. Schwede T., Kopp J., Guex N., Peitsch M.C. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Research 2003, 31:3381-3385.
29. Shiroishi M., Kuroki K., Rasubala L., Tsumoto K., Kumagai I., Kurimoto E., Kato K., Kohda D., Maenaka K. Structural basis for recognition of the nonclassical MHC molecule HLA-G by the leukocyte Ig-like receptor B2 (LILRB2/LIR2/ILT4/CD85d). Proceedings of the National Academy of Sciences of the United States of America 2006, 103:16412-16417.
30. 2-microglobulin, in vitro. Nature 1991, 350:619-622.
31. Theodossis A. On the trail of empty MHC class-I. Molecular Immunology 2013, 55:131-134.
32. Tugarinov V., Hwang P.M., Kay L.E. Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins. Annual Review of Biochemistry 2004, 73:107-146.
33. Wearsch P.A., Cresswell P. The quality control of MHC class I peptide loading. Current Opinion in Cell Biology 2008, 20:624-631.
34. Willcox B.E., Thomas L.M., Bjorkman P.J. Crystal structure of HLA-A2 bound to LIR-1, a host and viral major histocompatibility complex receptor. Nature Immunology 2003, 4:913-919.
35. Yagi-Utsumi M., Matsuo K., Yanagisawa K., Gekko K., Kato K. Spectroscopic characterization of intermolecular interaction of amyloid β promoted on GM1 micelles. International Journal of Alzheimer's Disease 2011, 2011:925073.
36. Yang J.T., Wu C.S., Martinez H.M. Calculation of protein conformation from circular dichroism. Methods in Enzymology 1986, 130:208-269.
37. 2 domain in peptide bound and free states: a molecular dynamics simulation study. Biophysical Journal 2004, 87:2203-2214.