Structure of the cross-β spine of amyloid-like fibrils
| العنوان: | Structure of the cross-β spine of amyloid-like fibrils |
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| المؤلفون: | Robert Grothe, Anders Ø. Madsen, Christian Riekel, Melinda Balbirnie, Rebecca Nelson, Michael R. Sawaya, David Eisenberg |
| المصدر: | Nature. 435:773-778 |
| بيانات النشر: | Springer Science and Business Media LLC, 2005. |
| سنة النشر: | 2005 |
| مصطلحات موضوعية: | Models, Molecular, Amyloid, Saccharomyces cerevisiae Proteins, Zipper, Prions, Molecular Sequence Data, Peptide, Saccharomyces cerevisiae, macromolecular substances, Crystallography, X-Ray, Fibril, Article, Protein Structure, Secondary, Protein structure, mental disorders, Side chain, Amino Acid Sequence, Peptide sequence, chemistry.chemical_classification, Multidisciplinary, Chemistry, Hydrogen Bonding, Amides, Peptide Fragments, Biochemistry, Structural biology, Biophysics, Thermodynamics, Crystallization, Peptide Termination Factors |
| الوصف: | Numerous soluble proteins convert to insoluble amyloid-like fibrils that have common properties. Amyloid fibrils are associated with fatal diseases such as Alzheimer's, and amyloid-like fibrils can be formed in vitro. For the yeast protein Sup35, conversion to amyloid-like fibrils is associated with a transmissible infection akin to that caused by mammalian prions. A seven-residue peptide segment from Sup35 forms amyloid-like fibrils and closely related microcrystals, from which we have determined the atomic structure of the cross-beta spine. It is a double beta-sheet, with each sheet formed from parallel segments stacked in register. Side chains protruding from the two sheets form a dry, tightly self-complementing steric zipper, bonding the sheets. Within each sheet, every segment is bound to its two neighbouring segments through stacks of both backbone and side-chain hydrogen bonds. The structure illuminates the stability of amyloid fibrils, their self-seeding characteristic and their tendency to form polymorphic structures. |
| تدمد: | 1476-4687 0028-0836 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5e9cfb4a7b77de3587f6de6ca57c51eTest https://doi.org/10.1038/nature03680Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....c5e9cfb4a7b77de3587f6de6ca57c51e |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14764687 00280836 |
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