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TitleThree-dimensional structure of human γ-secretase.
Journal, issue, pagesNature, Vol. 512, Issue 7513, Page 166-170, Year 2014
Publish dateAug 14, 2014
AuthorsPeilong Lu / Xiao-Chen Bai / Dan Ma / Tian Xie / Chuangye Yan / Linfeng Sun / Guanghui Yang / Yanyu Zhao / Rui Zhou / Sjors H W Scheres / Yigong Shi /
PubMed AbstractThe γ-secretase complex, comprising presenilin 1 (PS1), PEN-2, APH-1 and nicastrin, is a membrane-embedded protease that controls a number of important cellular functions through substrate cleavage. ...The γ-secretase complex, comprising presenilin 1 (PS1), PEN-2, APH-1 and nicastrin, is a membrane-embedded protease that controls a number of important cellular functions through substrate cleavage. Aberrant cleavage of the amyloid precursor protein (APP) results in aggregation of amyloid-β, which accumulates in the brain and consequently causes Alzheimer's disease. Here we report the three-dimensional structure of an intact human γ-secretase complex at 4.5 Å resolution, determined by cryo-electron-microscopy single-particle analysis. The γ-secretase complex comprises a horseshoe-shaped transmembrane domain, which contains 19 transmembrane segments (TMs), and a large extracellular domain (ECD) from nicastrin, which sits immediately above the hollow space formed by the TM horseshoe. Intriguingly, nicastrin ECD is structurally similar to a large family of peptidases exemplified by the glutamate carboxypeptidase PSMA. This structure serves as an important basis for understanding the functional mechanisms of the γ-secretase complex.
External linksNature / PubMed:25043039 / PubMed Central
MethodsEM (single particle)
Resolution4.5 - 5.4 Å
Structure data

EMDB-2677:
Three-dimensional structure of human gamma-secretase at 4.5 angstrom resolution
Method: EM (single particle) / Resolution: 4.5 Å

EMDB-2678:
Three-dimensional structure of human gamma-secretase at 5.4 angstrom resoltuion
Method: EM (single particle) / Resolution: 5.4 Å

Source
  • Homo sapiens (human)

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