Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Comment
. 2016 Aug 23;113(34):9398-400.
doi: 10.1073/pnas.1610806113. Epub 2016 Aug 9.

Implications for Alzheimer's disease of an atomic resolution structure of amyloid-β(1-42) fibrils

David S Eisenberg  1 , Michael R Sawaya  2
Affiliations
Comment

Implications for Alzheimer's disease of an atomic resolution structure of amyloid-β(1-42) fibrils

David S Eisenberg et al. Proc Natl Acad Sci U S A. .
No abstract available

PubMed Disclaimer

Conflict of interest statement

The authors declare no conflict of interest.

Figures

Fig. 1.
Fig. 1.
Comparison of two molecular models for amyloid-β(1–42) fibrils. (A) The near atomic resolution model determined by solid-state NMR by Wälti et al. (1). Two double-horseshoe–shaped molecules of amyloid-β(1–42) are shown (black and gray) related by a twofold axis (marked by a circle), which runs down the center of the fibril. The N-terminal 14 residues are disordered; one possible conformation is shown here by dotted lines. Many of the known familial mutations are carried by residues located on the outer surface (red). The surface hydrophobic patch formed by residues V40 and A42 (orange) may explain the greater rate of secondary nucleation by the 1–42 species compared with 1–40 (3). (B). The lower resolution (5–7 Å) model determined by Schmidt et al. (7) by cryo-EM is another polymorph of amyloid-β(1–42), also with two molecules per layer, related by a twofold axis, and also with a poorly ordered N terminus. The gray color represents a slice through the cryo-EM map. The two molecules appear to be related by a homo-steric zipper type of bonding. In both A and B the models are viewed down the fibril axis on the left and nearly perpendicular to the fibril axis on the right. (C) A hetero-zipper in amyloid-β(1–42) fibrils from Wälti et al. (1). (D) A homo-zipper from GNNQQNY (4). (E) A noncontiguous homo-zipper from Wälti et al. (1). Dotted lines represent intervening residues.
See this image and copyright information in PMC

Comment on

References

    1. Wälti MA, et al. Atomic resolution structure of a disease-relevant Aβ(1–42) amyloid fibril. Proc Natl Acad Sci USA. 2016;113:E4976–E4984. - PMC - PubMed
    1. Paravastu AK, Leapman RD, Yau W-M, Tycko R. Molecular structural basis for polymorphism in Alzheimer’s beta-amyloid fibrils. Proc Natl Acad Sci USA. 2008;105(47):18349–18354. - PMC - PubMed
    1. Colvin MT, et al. Atomic resolution structure of monomorphic Aβ42 amyloid fibrils. J Am Chem Soc. July 14, 2016 doi: 10.1021/jacs.6b05129. - DOI - PMC - PubMed
    1. Nelson R, et al. Structure of the cross-beta spine of amyloid-like fibrils. Nature. 2005;435(7043):773–778. - PMC - PubMed
    1. Sawaya MR, et al. Atomic structures of amyloid cross-beta spines reveal varied steric zippers. Nature. 2007;447(7143):453–457. - PubMed

LinkOut - more resources