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TitleFibril structure of amyloid-β(1-42) by cryo-electron microscopy.
Journal, issue, pagesScience, Vol. 358, Issue 6359, Page 116-119, Year 2017
Publish dateOct 6, 2017
AuthorsLothar Gremer / Daniel Schölzel / Carla Schenk / Elke Reinartz / Jörg Labahn / Raimond B G Ravelli / Markus Tusche / Carmen Lopez-Iglesias / Wolfgang Hoyer / Henrike Heise / Dieter Willbold / Gunnar F Schröder /
PubMed AbstractAmyloids 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 ...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.
External linksScience / PubMed:28882996 / PubMed Central
MethodsEM (helical sym.)
Resolution4.0 Å
Structure data

3851

5oqv

EMDB-3851, PDB-5oqv:
Near-atomic resolution fibril structure of complete amyloid-beta(1-42) by cryo-EM
Method: EM (helical sym.) / Resolution: 4.0 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / amyloid / fibril / aggregation / Alzheimer's disease

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