Crystallographic structure of a small molecule SIRT1 activator-enzyme complex

نویسندگان

  • Han Dai
  • April W Case
  • Thomas V Riera
  • Thomas Considine
  • Jessica E Lee
  • Yoshitomo Hamuro
  • Huizhen Zhao
  • Yong Jiang
  • Sharon M Sweitzer
  • Beth Pietrak
  • Benjamin Schwartz
  • Charles A Blum
  • Jeremy S Disch
  • Richard Caldwell
  • Bruce Szczepankiewicz
  • Christopher Oalmann
  • Pui Yee Ng
  • Brian H White
  • Rebecca Casaubon
  • Radha Narayan
  • Karsten Koppetsch
  • Francis Bourbonais
  • Bo Wu
  • Junfeng Wang
  • Dongming Qian
  • Fan Jiang
  • Cheney Mao
  • Minghui Wang
  • Erding Hu
  • Joe C Wu
  • Robert B Perni
  • George P Vlasuk
  • James L Ellis
چکیده

SIRT1, the founding member of the mammalian family of seven NAD(+)-dependent sirtuins, is composed of 747 amino acids forming a catalytic domain and extended N- and C-terminal regions. We report the design and characterization of an engineered human SIRT1 construct (mini-hSIRT1) containing the minimal structural elements required for lysine deacetylation and catalytic activation by small molecule sirtuin-activating compounds (STACs). Using this construct, we solved the crystal structure of a mini-hSIRT1-STAC complex, which revealed the STAC-binding site within the N-terminal domain of hSIRT1. Together with hydrogen-deuterium exchange mass spectrometry (HDX-MS) and site-directed mutagenesis using full-length hSIRT1, these data establish a specific STAC-binding site and identify key intermolecular interactions with hSIRT1. The determination of the interface governing the binding of STACs with human SIRT1 facilitates greater understanding of STAC activation of this enzyme, which holds significant promise as a therapeutic target for multiple human diseases.

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عنوان ژورنال:

دوره 6  شماره 

صفحات  -

تاریخ انتشار 2015