Structure of the cross-beta spine of amyloid-like fibrils. Nelson, R., Sawaya, M. R, Balbirnie, M., Madsen, A. Ø, Riekel, C., Grothe, R., & Eisenberg, D. Nature, 435(7043):773--8, June, 2005. ![Structure of the cross-beta spine of amyloid-like fibrils. [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex 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.
@article{nelson_structure_2005,
title = {Structure of the cross-beta spine of amyloid-like fibrils.},
volume = {435},
issn = {1476-4687},
shorttitle = {Nature},
url = {http://dx.doi.org/10.1038/nature03680},
doi = {10.1038/nature03680},
abstract = {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.},
number = {7043},
journal = {Nature},
author = {Nelson, Rebecca and Sawaya, Michael R and Balbirnie, Melinda and Madsen, Anders Ø and Riekel, Christian and Grothe, Robert and Eisenberg, David},
month = jun,
year = {2005},
pmid = {15944695},
keywords = {Amides, Amides: chemistry, Amino Acid Sequence, Amyloid, Amyloid: chemistry, Amyloid: metabolism, Crystallization, Crystallography, Hydrogen Bonding, Models, Molecular, Molecular Sequence Data, Peptide Fragments, Peptide Fragments: chemistry, Peptide Fragments: metabolism, Peptide Termination Factors, Prions, Prions: chemistry, Prions: metabolism, Protein Structure, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Saccharomyces cerevisiae Proteins: chemistry, Saccharomyces cerevisiae Proteins: metabolism, Saccharomyces cerevisiae: chemistry, Secondary, Thermodynamics, X-Ray},
pages = {773--8}
}
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