The parallel superpleated beta-structure as a model for amyloid fibrils of human amylin

Journal of Molecular Biology

Volumn 348, Issue 2, 2005, Pages 247-252

  Kajava, Andrey V ^a   Aebi, Ueli ^b   Steven, Alasdair C ^c  

^a Centre National de la Recherche Scientifique   (France)

^b UNIVERSITY OF BASEL   (Switzerland)

^c NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

Atomic structure; Diabetes mellitus; Fibrils; Islet amyloid; Molecular model

Indexed keywords

AMYLIN; AMYLOID; DISULFIDE; HYDROGEN; POLYPEPTIDE; PRION PROTEIN; PROTEIN URE2P; SERPENTINE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; DISULFIDE BOND; FIBER; HYDROGEN BOND; MOLECULAR MODEL; PEPTIDE ANALYSIS; PREDICTION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; PROTEIN VARIANT; RODENT; ROTATION; YEAST;

EID: 16244376187     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.02.029     Document Type: Article

References (37)

1. E. Opie The relation of diabetes mellitis to lesions of thepancreas. Hyaline degeneration of the islands of Langerhans J. Expt. Med. 5 1901 527 540
2. P. Westermark, and E. Wilander The influence of amyloid deposits on the islet volume in maturity onset diabetes mellitus Diabetologia 15 1978 417 421
3. H. King, R.E. Aubert, and W.H. Herman Global burden of diabetes, 1995-2025: prevalence, numerical estimates, and projections Diabetes Care 21 1998 1414 1431
4. M. Anguiano, R.J. Nowak, and P.T. Lansbury Jr Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes Biochemistry 41 2002 11338 11343
5. C. Goldsbury, K. Goldie, J. Pellaud, J. Seelig, P. Frey, and S.A. Muller Amyloid fibril formation from full-length and fragments of amylin J. Struct. Biol. 130 2000 352 362
6. A. Leckstrom, K. Bjorklund, J. Permert, R. Larsson, and P. Westermark Renal elimination of islet amyloid polypeptide Biochem. Biophys. Res. Commun. 239 1997 265 268
7. R. Kayed, J. Bernhagen, N. Greenfield, K. Sweimeh, H. Brunner, W. Voelter, and A. Kapurniotu Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in vitro J. Mol. Biol. 287 1999 781 796
8. P. Westermark, U. Engstrom, K.H. Johnson, G.T. Westermark, and C. Betsholtz Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation Proc. Natl Acad. Sci. USA 87 1990 5036 5040
9. M.R. Nilsson, and D.P. Raleigh Analysis of amylin cleavage products provides new insights into the amyloidogenic region of human amylin J. Mol. Biol. 294 1999 1375 1385
10. S.B. Charge, E.J. de Koning, and A. Clark Effect of pH and insulin on fibrillogenesis of islet amyloid polypeptide in vitro Biochemistry 34 1995 14588 14593
11. E.T. Jaikaran, C.E. Higham, L.C. Serpell, J. Zurdo, M. Gross, A. Clark, and P.E. Fraser Identification of a novel human islet amyloid polypeptide beta-sheet domain and factors influencing fibrillogenesis J. Mol. Biol. 308 2001 515 525
12. C.S. Goldsbury, G.J. Cooper, K.N. Goldie, S.A. Muller, E.L. Saafi, and W.T. Gruijters Polymorphic fibrillar assembly of human amylin J. Struct. Biol. 119 1997 17 27
13. S.O. Makin, and L.C. Serpell Structural characterisation of islet amyloid polypeptide fibrils J. Mol. Biol. 335 2004 1279 1288
14. J.J. Balbach, Y. Ishii, O.N. Antzutkin, R.D. Leapman, N.W. Rizzo, and F. Dyda Amyloid fibril formation by A beta 16-22, a seven-residue fragment of the Alzheimer's beta-amyloid peptide, and structural characterization by solid state NMR Biochemistry 39 2000 13748 13759
15. J.M. Griffiths, T.T. Ashburn, M. Auger, P.R. Costa, R.G. Griffin, and P.T. Lansbury Rotational resonance solid-state NMR elucidates a structural model of pancreatic amyloid J. Am. Chem. Soc. 117 1995 3539 3546
16. E.T. Jaikaran, and A. Clark Islet amyloid and type 2 diabetes: from molecular misfolding to islet pathophysiology Biochim. Biophys. Acta 1537 2001 179 203
17. S.A. Jayasinghe, and R. Langen Identifying structural features of fibrillar islet amyloid polypeptide using site-directed spin labeling J. Biol. Chem. 279 2004 48420 48425
18. A.V. Kajava, U. Baxa, R.B. Wickner, and A.C. Steven A model for Ure2p prion filaments and other amyloids: The parallel superpleated beta-structure Proc. Natl Acad. Sci. USA 101 2004 7885 7890
19. L. Pauling, and R.B. Corey Stable configurations of polypeptide chains Proc. Roy. Soc. ser. B 141 1953 21 33
20. C. Goldsbury, J. Kistler, U. Aebi, T. Arvinte, and G.J. Cooper Watching amyloid fibrils grow by time-lapse atomic force microscopy J. Mol. Biol. 285 1999 33 39
21. S.B. Padrick, and A.D. Miranker Islet amyloid polypeptide: identification of long-range contacts and local order on the fibrillogenesis pathway J. Mol. Biol. 308 2001 783 794
22. M.D. Yoder, N.T. Keen, and F. Jurnak New domain motif: the structure of pectate lyase C, a secreted plant virulence factor Science 260 1993 1503 1507
23. E.J. de Koning, N.L. Bodkin, B.C. Hansen, and A. Clark Diabetes mellitus in Macaca mulatta monkeys is characterised by islet amyloidosis and reduction in beta-cell population Diabetologia 36 1993 378 384
24. B.L. Yano, D.W. Hayden, and K.H. Johnson Feline insular amyloid. Ultrastructural evidence for intracellular formation by nonendocrine cells Lab. Invest. 45 1981 149 156
25. J. Green, C. Goldsbury, T. Mini, S. Sunderji, P. Frey, and J. Kistler Full-length rat amylin forms fibrils following substitution of single residues from human amylin J. Mol. Biol. 326 2003 1147 1156
26. S.C. Lee, Y. Hashim, J.K. Li, G.T. Ko, J.A. Critchley, C.S. Cockram, and J.C. Chan The islet amyloid polypeptide (amylin) gene S20G mutation in Chinese subjects: evidence for associations with type 2 diabetes and cholesterol levels Clin. Endocrinol. (Oxford) 54 2001 541 546
27. K. Johansson, M. El-Ahmad, R. Friemann, H. Jornvall, O. Markovic, and H. Eklund Crystal structure of plant pectin methylesterase FEBS Letters 514 2002 243 249
28. S. Steinbacher, R. Seckler, S. Miller, B. Steipe, R. Huber, and P. Reinemer Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer Science 265 1994 383 386
29. P. Emsley, I.G. Charles, N.F. Fairweather, and N.W. Isaacs Structure of Bordetella pertussis virulence factor P.69 pertactin Nature 381 1996 90 92
30. J.D. Green, C. Goldsbury, J. Kistler, G.J. Cooper, and U. Aebi Human amylin oligomer growth and fibril elongation define two distinct phases in amyloid formation J. Biol. Chem. 279 2004 12206 12212
31. E.N. Baker, and R.E. Hubbard Hydrogen bonding in globular proteins Prog. Biophys. Mol. Biol. 44 1984 97 179
32. S.J. Wimalawansa Amylin, calcitonin gene-related peptide, calcitonin, and adrenomedullin: a peptide superfamily Crit. Rev. Neurobiol. 11 1997 167 239
33. 13C solid-state NMR spectroscopy Magn. Reson. Chem. 42 2004 247 257
34. H.H. Bauer, U. Aebi, M. Haner, R. Hermann, M. Muller, and H.P. Merkle Architecture and polymorphism of fibrillar supramolecular assemblies produced by in vitro aggregation of human calcitonin J. Struct. Biol. 115 1995 1 15
35. G. Andreotti, and A. Motta Modulating calcitonin fibrillogenesis: an antiparallel alpha-helical dimer inhibits fibrillation of salmon calcitonin J. Biol. Chem. 279 2004 6364 6370
36. H.E. Dayring, A. Tramonato, S.R. Sprang, and R.J. Fletterick Interactive program for visualization and modeling of proteins, nucleic acids and small molecules J. Mol. Graph. 4 1986 82 87
37. R.A. Laskowski, M.W. McArthur, D.S. Moss, and J.M. Thornton PROCHECK: a program to check the stereochemical quality of protein structures J. Appl. Crystallog. 26 1993 282 291