TY  - JOUR
AU  - Gremer, Lothar
AU  - Schölzel, Daniel
AU  - Schenk, Carla
AU  - Reinartz, Elke
AU  - Labahn, Jörg
AU  - Ravelli, Raimond B. G.
AU  - Tusche, Markus
AU  - Lopez-Iglesias, Carmen
AU  - Hoyer, Wolfgang
AU  - Heise, Henrike
AU  - Willbold, Dieter
AU  - Schröder, Gunnar
TI  - Fibril structure of amyloid-ß(1-42) by cryoelectron microscopy
JO  - Science
VL  - 358
SN  - 0036-8075
CY  - Washington, DC [u.a.]
PB  - American Association for the Advancement of Science
M1  - FZJ-2017-06585
SP  - 116-119
PY  - 2017
N1  - Journal title: Science
AB  - 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 cryoelectron microscopy (cryo-EM) to 4.0 Å resolution, complemented by solid-state nuclear magnetic resonance (NMR) experiments. The backbone of all 42 residues and nearly all sidechains 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 unique 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.
LB  - PUB:(DE-HGF)16
C6  - pmid:28882996
UR  - <Go to ISI:>//WOS:000412359600065
DO  - DOI:10.1126/science.aao2825
UR  - https://juser.fz-juelich.de/record/837796
ER  -