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TitleStructural interactions between inhibitor and substrate docking sites give insight into mechanisms of human PS1 complexes.
Journal, issue, pagesStructure, Vol. 22, Issue 1, Page 125-135, Year 2014
Publish dateJan 7, 2014
AuthorsYi Li / Stephen Hsueh-Jeng Lu / Ching-Ju Tsai / Christopher Bohm / Seema Qamar / Roger B Dodd / William Meadows / Amy Jeon / Adam McLeod / Fusheng Chen / Muriel Arimon / Oksana Berezovska / Bradley T Hyman / Taisuke Tomita / Takeshi Iwatsubo / Christopher M Johnson / Lindsay A Farrer / Gerold Schmitt-Ulms / Paul E Fraser / Peter H St George-Hyslop /
PubMed AbstractPresenilin-mediated endoproteolysis of transmembrane proteins plays a key role in physiological signaling and in the pathogenesis of Alzheimer disease and some cancers. Numerous inhibitors have been ...Presenilin-mediated endoproteolysis of transmembrane proteins plays a key role in physiological signaling and in the pathogenesis of Alzheimer disease and some cancers. Numerous inhibitors have been found via library screens, but their structural mechanisms remain unknown. We used several biophysical techniques to investigate the structure of human presenilin complexes and the effects of peptidomimetic γ-secretase inhibitors. The complexes are bilobed. The head contains nicastrin ectodomain. The membrane-embedded base has a central channel and a lateral cleft, which may represent the initial substrate docking site. Inhibitor binding induces widespread structural changes, including rotation of the head and closure of the lateral cleft. These changes block substrate access to the catalytic pocket and inhibit the enzyme. Intriguingly, peptide substrate docking has reciprocal effects on the inhibitor binding site. Similar reciprocal shifts may underlie the mechanisms of other inhibitors and of the "lateral gate" through which substrates access to the catalytic site.
External linksStructure / PubMed:24210759 / PubMed Central
MethodsEM (single particle)
Resolution17.4 Å
Structure data

EMDB-2477:
Negative stain electron microscopy structure of native human Presenilin 1 (PS1) complex
Method: EM (single particle) / Resolution: 17.4 Å

EMDB-2478:
Negative stain electron microscopy structure of compound E-bound human Presenilin 1 (PS1) complex
Method: EM (single particle) / Resolution: 17.4 Å

Source
  • Homo sapiens (human)
  • synthetic construct (others)

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