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TitleCryo-EM structures of amyloid-β filaments with the Arctic mutation (E22G) from human and mouse brains.
Journal, issue, pagesActa Neuropathol, Vol. 145, Issue 3, Page 325-333, Year 2023
Publish dateJan 7, 2023
AuthorsYang Yang / Wenjuan Zhang / Alexey G Murzin / Manuel Schweighauser / Melissa Huang / Sofia Lövestam / Sew Y Peak-Chew / Takashi Saito / Takaomi C Saido / Jennifer Macdonald / Isabelle Lavenir / Bernardino Ghetti / Caroline Graff / Amit Kumar / Agneta Nordberg / Michel Goedert / Sjors H W Scheres /
PubMed AbstractThe Arctic mutation, encoding E693G in the amyloid precursor protein (APP) gene [E22G in amyloid-β (Aβ)], causes dominantly inherited Alzheimer's disease. Here, we report the high-resolution cryo- ...The Arctic mutation, encoding E693G in the amyloid precursor protein (APP) gene [E22G in amyloid-β (Aβ)], causes dominantly inherited Alzheimer's disease. Here, we report the high-resolution cryo-EM structures of Aβ filaments from the frontal cortex of a previously described case (AβPParc1) with the Arctic mutation. Most filaments consist of two pairs of non-identical protofilaments that comprise residues V12-V40 (human Arctic fold A) and E11-G37 (human Arctic fold B). They have a substructure (residues F20-G37) in common with the folds of type I and type II Aβ42. When compared to the structures of wild-type Aβ42 filaments, there are subtle conformational changes in the human Arctic folds, because of the lack of a side chain at G22, which may strengthen hydrogen bonding between mutant Aβ molecules and promote filament formation. A minority of Aβ42 filaments of type II was also present, as were tau paired helical filaments. In addition, we report the cryo-EM structures of Aβ filaments with the Arctic mutation from mouse knock-in line App. Most filaments are made of two identical mutant protofilaments that extend from D1 to G37 (App murine Arctic fold). In a minority of filaments, two dimeric folds pack against each other in an anti-parallel fashion. The App murine Arctic fold differs from the human Arctic folds, but shares some substructure.
External linksActa Neuropathol / PubMed:36611124 / PubMed Central
MethodsEM (helical sym.)
Resolution1.99 - 3.5 Å
Structure data

16022

8bfz

EMDB-16022, PDB-8bfz:
Amyloid-beta 42 filaments extracted from the human brain with Arctic mutation (E22G) of Alzheimer's disease | ABeta42
Method: EM (helical sym.) / Resolution: 2.8 Å

16023

8bg0

EMDB-16023, PDB-8bg0:
Amyloid-beta tetrameric filaments with the Arctic mutation (E22G) from Alzheimer's disease brains | ABeta40
Method: EM (helical sym.) / Resolution: 1.99 Å

16027

8bg9

EMDB-16027, PDB-8bg9:
Murine amyloid-beta filaments with the Arctic mutation (E22G) from APP(NL-G-F) mouse brains | ABeta
Method: EM (helical sym.) / Resolution: 3.5 Å

Chemicals

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
  • human (human)
  • mus musculus (house mouse)
  • house mouse (house mouse)
KeywordsPROTEIN FIBRIL / Amyloid / filaments / amyloid-beta / Arctic mutation / APP / E22G / E693G / NL-G-F / mouse brains

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