Solution structure of β2-microglobulin and insights into fibrillogenesis

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1753, Issue 1, 2005, Pages 76-84

  Esposito, Gennaro ^a   Corazza, Alessandra ^a   Viglino, Paolo ^a   Verdone, Giuliana ^a   Pettirossi, Fabio ^a   Fogolari, Federico ^a   Makek, Ads ^a   Giorgetti, Sofia ^b   Mangione, Palma ^b   Stoppini, Monica ^b   Bellotti, Vittorio ^b  

^a UNIVERSITY OF UDINE   (Italy)

^b UNIVERSITY OF PAVIA   (Italy)

Author keywords

2 microglobulin mutant; 2 microglobulin NMR structure; 2 microglobulin conformation; 2 microglobulin solution structure; Amyloidogenic protein NMR; Protein NMR

Indexed keywords

AMYLOID; BETA 2 MICROGLOBULIN; COPPER; IMIDAZOLE; PROTEIN;

CALCULATION; CONFERENCE PAPER; CRYSTAL STRUCTURE; FIBRILLOGENESIS; HEAVY CHAIN; HUMAN; MAJOR HISTOCOMPATIBILITY COMPLEX; MUTANT; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN METABOLISM; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; PROTON TRANSPORT; SOLVATION; STRUCTURE ANALYSIS; SURFACE CHARGE; TITRIMETRY; WILD TYPE;

AMYLOID; BETA 2-MICROGLOBULIN; CRYSTALLOGRAPHY, X-RAY; DRUG STABILITY; EVOLUTION, MOLECULAR; HUMANS; MODELS, MOLECULAR; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; SOLUTIONS; THERMODYNAMICS;

EID: 27744552294     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.07.003     Document Type: Conference Paper

References (34)

1. F. Gejyo, T. Yamada, S. Odani, Y. Nakagawa, M. Arakawa, T. Kunitomo, H. Kataoka, M. Suzuki, Y. Hirasawa, T. Shirahama, A.S. Cohen, and K. Schmid A new form of amyloid protein associated with hemodialysis was identified as β2-microglobulin Biochem. Biophys. Res. Commun. 129 1985 701 706
2. J. Flöge, and M. Ketteler β2-microglobulin-derived amyloidosis: an update Kidney Int. 59 2001 164 171
3. P.J. Bjorkman, J.L. Strominger, and D.C. Wiley Crystallization and X-ray diffraction studies on the histocompatibility antigens HLA-A2 and HLA-A28 from human cell membranes J. Mol. Biol. 186 1985 205 210
4. P.J. Bjorkman, M.A. Saper, B. Samaroui, W.S. Bennet, J.L. Strominger, and D.C. Wiley Structure of the human class I histocompatibility antigen, HLA-A2 Nature 329 1987 506 512
5. M.A. Saper, P.J. Bjorkman, and D.C. Wiley Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution J. Mol. Biol. 219 1991 277 319
6. J.W. Becker, and G.N. Reeke Jr. Three-dimensional structure of β2-microglobulin Proc. Nat. Acad. Sci. U. S. A. 82 1985 4225 4229
7. 1H NMR assignments and secondary structure of human β2-microglobulin in solution Biochemistry 31 1992 8906 8915
8. K. Wüthrich NMR Spectroscopy Of Proteins and Nucleic Acids 1986 Wiley and Sons New York
9. V. Bellotti, M. Stoppini, P. Mangione, M. Sunde, C.V. Robinson, L. Asti, D. Brancaccio, and G. Ferri β2-microglobulin can be refolded into a native state from ex vivo amyloid fibrils Eur. J. Biochem. 258 1998 61 67
10. G. Esposito, R. Michelutti, G. Verdone, P. Viglino, H. Hernández, C.V. Robinson, A. Amoresano, F. Dal Piaz, M. Monti, P. Pucci, P. Mangione, L. Asti, M. Stoppini, G. Merlini, G. Ferri, and V. Bellotti Removal of the N-terminal hexapeptide from human β2-microglobulin facilitates protein aggregation and fibril formation Protein Sci. 9 2000 831 845
11. D.S. Wishart, and B.D. Sykes Chemical shifts as a tool for structure determination Methods Enzymol. 239 1994 363 392
12. R. Koradi, M. Billeter, and K. Wüthrich MOLMOL a program for display and analysis of macromolecular structure J. Mol. Graphics 14 1996 51 55
13. 2-microglobulin amyloid fibril by H/D exchange Nat. Struct. Biol. 9 2002 332 336
14. 2-microglobulin Nat. Struct. Biol. 9 2002 326 331
15. Y.K. Cheng, and P.J. Rossky Surface topography dependence of biomolecular hydrophobic hydration Nature 392 1998 696 699
16. G. Verdone, A. Corazza, P. Viglino, F. Pettirossi, S. Giorgetti, P. Mangione, A. Andreola, M. Stoppini, V. Bellotti, and G. Esposito The solution structure of β2-microglobulin reveals the prodromes of its amyloid transition Protein Sci. 11 2002 487 499
17. W. Kabsh, and C. Sander Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features Biopolymers 22 1983 2577 2637
18. J. Antosiewicz, J.A. McCammon, and M.K. Gilson Prediction of pH-dependent properties of proteins J. Mol. Biol. 238 1994 415 436
19. J.D. Madura, J.M. Briggs, R. Wade, M.E. Davis, B.A. Luty, A. Ilin, J. Antosiewicz, M.K. Gilson, B. Bagheri, L. Ridgway Scott, and J.A. McCammon Electrostatics and diffusion of molecules in solution: simulations with the University of Houston Brownian Dynamics program Comput. Commun. Phys. 91 1995 57 95
20. T. Ward, and R.T. Steigbigel Acidosis of synovial fluids correlates with synovial fluid leukocytosis Am. J. Med. 64 1978 933 936
21. C.J. Morgan, M. Gelfand, C. Atreya, and A.D. Miranker Kidney dialysis-associated amyloidosis: a molecular role for copper in fiber formation J. Mol. Biol. 309 2001 339 345
22. 2-microglobulin Biochemistry 41 2002 10646 10656
23. 2- microglobulin upon copper binding: a possible role for copper in dialysis-related amyloidosis Protein Sci. 13 2004 797 809
24. 2-microglobulin reveals clues to its amyloidogenic properties Proc. Natl. Acad. Sci. U. S. A. 99 2002 9771 9776
25. J.S. Richardson, and D.C. Richrdson Natural b-sheet proteins use negative design to avoid edge-to-edge aggregation Proc. Natl. Acad. Sci. U. S. A. 99 2002 2754 2759
26. R.A. Laskowski, J.A.C. Rullmann, M.W. MacArthur, R. Kaptein, and J.M. Thornton AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR J. Biomol. NMR 8 1996 477 486
27. E. De Lorenzi, S. Grossi, G. Massolini, S. Giorgetti, P. Mangione, A. Andreola, F. Chiti, V. Bellotti, and G. Caccialanza Capillary electrophoresis investigation of a partially unfolded conformation of β2-microglobulin Electophoresis 23 2002 918 925
28. 2-microglobulin and amyloidogenesis J. Biol. Chem. 279 2004 9176 9189
29. C. Rosano, S. Zuccotti, P. Mangione, S. Giorgetti, V. Bellotti, F. Pettirossi, A. Corazza, P. Viglino, G. Esposito, and M. Bolognesi β2-microglobulin H31Y variant 3D-structure highlights the protein natural propensity towards intermolecular aggregation J. Mol. Biol. 330 2003 1051 1064
30. 2-microglobulin: results from X-ray crystallography Biochim. Biophys. Acta 1753 2005 97 103 doi:10.1016/j.bbapap.2005.07.010
31. 2- microglobulin J. Mol. Biol. 307 2001 379 391
32. 2-microglobulin is significantly populated under physiological conditions and involved in fibrillogenesis J. Biol. Chem. 276 2001 46714 46721
33. 2-microglobulin trapped by non-native prolyl peptide bond J. Mol. Biol. 348 2005 383 397
34. T.R. Serio, A.G. Cashikar, A.S. Kowal, G.J. Savicki, J.J. Moslehi, L. Serpell, M.F. Arnsdorf, and S.L. Lindquist Nucleated conformational conversion and the replication of conformational information by a prion determinant Science 289 2000 1317 1321