Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 105, Issue 21, Pages 7462-7466Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0712290105
Keywords
Alzheimer's disease; amyloid-beta; electron cryomicroscopy; neurodegeneration; protein folding
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Funding
- Howard Hughes Medical Institute Funding Source: Medline
- NIGMS NIH HHS [P01 GM062580, 1 P01 GM-62580] Funding Source: Medline
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Alzheimer's disease is a neurodegenerative disorder that is characterized by the cerebral deposition of amyloid fibrils formed by A(beta) peptide. Despite their prevalence in Alzheimer's and other neurodegenerative diseases, important details of the structure of amyloid fibrils remain unknown. Here, we present a three-dimensional structure of a mature amyloid fibril formed by A beta(1-40) peptide, determined by electron cryomicroscopy at approximate to 8-angstrom resolution. The fibril consists of two protofilaments, each containing approximate to 5-nm-long regions of beta-sheet structure. A local twofold symmetry within each region suggests that pairs of beta-sheets are formed from equivalent parts of two A beta(1-40) peptides contained in each protofilament. The pairing occurs via tightly packed interfaces, reminiscent of recently reported steric zipper structures. However, unlike these previous structures, the beta-sheet pairing is observed within an amyloid fibril and includes significantly longer amino acid sequences.
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