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TitleRecognition of the amyloid precursor protein by human γ-secretase.
Journal, issue, pagesScience, Vol. 363, Issue 6428, Year 2019
Publish dateFeb 15, 2019
AuthorsRui Zhou / Guanghui Yang / Xuefei Guo / Qiang Zhou / Jianlin Lei / Yigong Shi /
PubMed AbstractCleavage of amyloid precursor protein (APP) by the intramembrane protease γ-secretase is linked to Alzheimer's disease (AD). We report an atomic structure of human γ-secretase in complex with a ...Cleavage of amyloid precursor protein (APP) by the intramembrane protease γ-secretase is linked to Alzheimer's disease (AD). We report an atomic structure of human γ-secretase in complex with a transmembrane (TM) APP fragment at 2.6-angstrom resolution. The TM helix of APP closely interacts with five surrounding TMs of PS1 (the catalytic subunit of γ-secretase). A hybrid β sheet, which is formed by a β strand from APP and two β strands from PS1, guides γ-secretase to the scissile peptide bond of APP between its TM and β strand. Residues at the interface between PS1 and APP are heavily targeted by recurring mutations from AD patients. This structure, together with that of γ-secretase bound to Notch, reveal contrasting features of substrate binding, which may be applied toward the design of substrate-specific inhibitors.
External linksScience / PubMed:30630874
MethodsEM (single particle)
Resolution2.6 Å
Structure data

9751

6iyc

EMDB-9751, PDB-6iyc:
Recognition of the Amyloid Precursor Protein by Human gamma-secretase
Method: EM (single particle) / Resolution: 2.6 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-PC1:
1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipid*YM / Phosphatidylcholine

ChemComp-CLR:
CHOLESTEROL / Cholesterol

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / Complex

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