The three-dimensional structure of β2 microglobulin: Results from X-ray crystallography

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1753, Issue 1, 2005, Pages 85-91

  Rosano, Camillo ^a   Zuccotti, Simone ^b   Bolognesi, Martino ^b,c  

^a UNIVERSITY OF GENOA   (Italy)

^b UNIVERSITY OF GENOA   (Italy)

^c UNIVERSITY OF MILAN   (Italy)

Author keywords

2 microglobulin; Amyloid fibril; Class I major histocompatibility complex; Cross structure; Dialysis related amyloidosis

Indexed keywords

AMYLOID; BETA 2 MICROGLOBULIN; IMMUNOGLOBULIN;

AMYLOIDOSIS; CONFERENCE PAPER; CRYSTAL STRUCTURE; DIALYSIS; DIALYSIS RELATED AMYLOIDOSIS; HEAVY CHAIN; HUMAN; JOINT; LIGHT CHAIN; MAJOR HISTOCOMPATIBILITY COMPLEX; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DEGRADATION; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY; AMINO ACID SEQUENCE; ANIMAL; CATTLE; CHEMISTRY; GENETICS; PROTEIN SECONDARY STRUCTURE; RENAL REPLACEMENT THERAPY; REVIEW; SEQUENCE ALIGNMENT;

AMINO ACID SEQUENCE; AMYLOID; AMYLOIDOSIS; ANIMALS; BETA 2-MICROGLOBULIN; CATTLE; CRYSTALLOGRAPHY, X-RAY; HUMANS; PROTEIN STRUCTURE, SECONDARY; RENAL DIALYSIS; SEQUENCE ALIGNMENT;

EID: 27744499225     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.07.010     Document Type: Conference Paper

References (30)

1. J. Floege, and G. Ehlerding β2-microglobulin associated amyloidosis Nephron 72 1996 9 26
2. 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 chronic hemodialysis was identified as beta 2-microglobulin Biochem. Biophys. Res. Commun. 129 1985 701 706
3. R.P. Linke, A. Kerling, and A. Rail Hemodialysis: demonstration of truncated β2-microglobulin in AB-amyloid in situ Kidney Inter., Suppl. 41 1993 100 105
4. 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
5. C.H. Trinh, D.P. Smith, A.P. Kalverda, S.E. Phillips, and S.E. Radford Crystal structure of monomeric human β2-microglobulin reveals clues to its amyloidogenic properties Proc. Natl. Acad. Sci. U. S. A. 99 2002 9771 9776
6. J.S. Richardson, and D.C. Richardson Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation Proc. Natl. Acad. Sci. U. S. A. 99 2002 2754 2759
7. M.R. Krebs, L.A. Morozova-Roche, K. Daniel, C.V. Robinson, and C.M. Dobson Observation of sequence specificity in the seeding of protein amyloid fibrils Protein Sci. 13 7 2004 1933 1938
8. N.H. Heegaard, T.J. Jorgensen, N. Rozlosnik, D.B. Corlin, J.S. Pedersen, A.G. Tempesta, P. Roepstorff, R. Bauer, and M.H. Nissen Unfolding, aggregation, and seeded amyloid formation of lysine-58-cleaved β2-microglobulin Biochemistry 44 11 2005 4397 4407
9. A. Kameda, M. Hoshino, T. Higurashi, S. Takahashi, H. Naiki, and Y. Goto J. Mol. Biol. 348 2005 383 397
10. H. Naiki, N. Hashimoto, S. Suzuki, H. Kimura, K. Nakakuki, and F. Gejyo Establishment of a kinetic model of dialysis-related amyloid fibril extension in vitro Amyloid Int. J. Exp. Clin. Invest. 4 1997 223 232
11. V.J. McParland, N.M. Kad, A.P. Kalverda, A. Brown, P. Kirwin-Jones, M.G. Hunter, M. Sunde, and S.E. Radford Partially unfolded states of β2-microglobulin and amyloid formation in vitro Biochemistry 39 2000 8735 8746
12. N.M. Kad, N.H. Thomson, D.P. Smith, D.A. Smith, and S.E. Radford β2-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro J. Mol. Biol. 313 3 2001 559 571
13. A.J. Borysik, S.E. Radford, and A.E. Ashcroft Co-populated conformational ensembles of β2-microglobulin uncovered quantitatively by electrospray ionization mass spectrometry J. Biol. Chem. 279 2004 27069 27077
14. L.H. Connors, T. Shirahama, M. Skinner, A. Fenves, and A.S. Cohen In vitro formation of amyloid fibrils from intact β2-microglobulin Biochem. Biophys. Res. Commun. 131 1995 1063 1068
15. F. Chiti, P. Mangione, A. Andreola, S. Giorgetti, M. Stefani, C.M. Dobson, V. Bellotti, and N. Taddei Detection of two partially structured species in the folding process of the amyloidogenic protein β2-microglobulin J. Mol. Biol. 307 2001 379 391
16. S. Yamamoto, K. Hasegawa, I. Yamaguchi, S. Tsutsumi, J. Kardos, Y. Goto, F. Gejyo, and H. Naiki Low concentrations of sodium dodecyl sulfate induce the extension of beta 2-microglobulin-related amyloid fibrils at a neutral pH Biochemistry 43 2005 11075 11082
17. 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 human β2-microglobulin reveals the prodromes of its amyloid transition Protein Sci. 11 2002 487 499
18. G. Esposito, R. Michelutti, G. Verdone, P. Viglino, H. Hernández, C.V. Robonson, A. Amoresano, F. Dal Piaz, M. Monti, P. Pucci, P. Mangione, 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
19. H.M. Berman, J. Westbrook, Z. Feng, G. Gillilang, T.N. Bhat, and M. Weisseg The protein data bank Nucleic Acids Res. 28 2000 235 242
20. J.W. Becker, and G.N. Reeke Jr. Three-dimensional structure of beta 2-microglobulin Proc. Natl. Acad. Sci. U. S. A. 82 12 1985 4225 4229
21. 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. 335 4 2004 1051 1064
22. M. Okon, P. Bray, and D. Vucelic 1H NMR assignments and secondary structure of human β2-microglobulin in solution Biochemistry 31 1992 8906 8915
23. M. Hoshino, H. Katou, Y. Hagihara, K. Hasegawa, H. Naiki, and Y. Goto Mapping of the core of the β2-microglobulin amyloid fibril by H/D exchange Nat. Struct. Biol. 9 2002 332 336
24. V.J. McParland, A.P. Kalverda, S.W. Homans, and S.E. Radford Structural properties of an amyloid precursor of β2-microglobulin Nat. Struct. Biol. 9 2002 326 331
25. P.J. Bjorkman, M.A. Saper, B. Samraoui, W.S. Bennett, J.L. Strominger, and D.C. Wiley Structure of the human class I histocompatibility antigen, HLA-A2 Nature 329 1987 506 512
26. M.A. Saper, P.J. Bjorkman, and D.C. Wiley Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 A resolution J. Mol. Biol. 219 1991 277 319
27. J.W. Becker, J.A. Ziffer, G.M. Edelman, and B.A. Cunningham Crystallographic studies of bovine beta2-microglobulin Proc. Natl. Acad. Sci. U. S. A. 74 8 1997 3345 3349
28. 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 Electrophoresis 23 2002 918 925
29. S. Zuccotti, C. Rosano, P. Mangione, V. Bellotti, and M. Bolognesi Preliminary crystallographic characterization of the human β2-microglobulin His31Tyr mutant in a tetrameric assembly Acta Crystallogr., D Biol. Crystallogr. 59 2003 1270 1272
30. M. Monti, S. Principe, S. Giorgetti, P. Mangione, G. Merlini, A. Clark, V. Bellotti, A. Amoresano, and P. Pucci Topological investigation of amyloid fibrils obtained from β2-microglobulin Protein Sci. 11 2002 2362 2369