Journal Article

PUBDB-2024-01052

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Fibril structure of amyloid-β(1–42) by cryo–electron microscopy

Gremer, L. ; Schölzel, D. ; Schenk, C. ; Reinartz, E. ; Labahn, J.CSSB* ; Ravelli, R. B. G. ; Tusche, M. ; Lopez-Iglesias, C. ; Hoyer, W. ; Heise, H. ; Willbold, D. (Corresponding author) ; Schröder, G. F. (Corresponding author)

2017
Assoc. Washington, DC

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Please use a persistent id in citations: doi:10.1126/science.aao2825

Abstract: Amyloids are implicated in neurodegenerative diseases. Fibrillar aggregates of the amyloid-β protein (Aβ) are the main component of the senile plaques found in brains of Alzheimer’s disease patients. We present the structure of an Aβ(1–42) fibril composed of two intertwined protofilaments determined by cryo–electron microscopy (cryo-EM) to 4.0-angstrom resolution, complemented by solid-state nuclear magnetic resonance experiments. The backbone of all 42 residues and nearly all side chains are well resolved in the EM density map, including the entire N terminus, which is part of the cross-β structure resulting in an overall “LS”-shaped topology of individual subunits. The dimer interface protects the hydrophobic C termini from the solvent. The characteristic staggering of the nonplanar subunits results in markedly different fibril ends, termed “groove” and “ridge,” leading to different binding pathways on both fibril ends, which has implications for fibril growth.

Note: ISSN 1095-9203 not unique: **3 hits**.

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Contributing Institute(s):

1. CSSB-FZJ-JL (CSSB-FZJ-JL)

Research Program(s):

1. 899 - ohne Topic (POF4-899) (POF4-899)
2. BETACONTROL - Control of amyloid formation via beta-hairpin molecular recognition features (726368) (726368)

Experiment(s):

1. No specific instrument

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