Infectious and noninfectious amyloids of the HET-s(218-289) prion have different NMR spectra

被引:40
作者
Wasmer, Christian [1 ]
Soragni, Alice [1 ]
Sabate, Raimon [2 ]
Lange, Adam [1 ]
Riek, Roland [1 ]
Meier, Beat H. [1 ]
机构
[1] ETH, Phys Chem Lab, CH-8093 Zurich, Switzerland
[2] Univ Bordeaux 2, Lab Genet Mol Champignons, IBGC UMR CNRS 5095, F-33076 Bordeaux, France
关键词
amyloids; fibrils; NMR spectroscopy; protein structures; structural biology;
D O I
10.1002/anie.200704896
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
(Graph Presented) The molecular basis for prion infectivity is not yet understood. The NMR spectra of noninfectious and infectious amyloids of the prion-forming domain 218-289 of the fungal prion HET-s are clearly different (see picture) but are indicative for a cross-β arrangement in both cases. The fibrils formed at pH 3 are not infectious because their molecular structure apparently differs substantially from that formed at physiological pH. © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.
引用
收藏
页码:5839 / 5841
页数:3
相关论文
共 23 条
[21]   Observation of highly flexible residues in amyloid fibrils of the HET-s prion [J].
Siemer, Ansgar B. ;
Arnold, Alexandre A. ;
Ritter, Christiane ;
Westfeld, Thomas ;
Ernst, Matthias ;
Riek, Roland ;
Meier, Beat H. .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2006, 128 (40) :13224-13228
[22]   EMPIRICAL CORRELATION BETWEEN PROTEIN BACKBONE CONFORMATION AND C-ALPHA AND C-BETA C-13 NUCLEAR-MAGNETIC-RESONANCE CHEMICAL-SHIFTS [J].
SPERA, S ;
BAX, A .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1991, 113 (14) :5490-5492
[23]   The structural basis of yeast prion strain variants [J].
Toyama, Brandon H. ;
Kelly, Mark J. S. ;
Gross, John D. ;
Weissman, Jonathan S. .
NATURE, 2007, 449 (7159) :233-U8