Abstract:
: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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Dai H,Case AW,Riera TV,Considine T,Lee JE,Hamuro Y,Zhao H,Jiang Y,Sweitzer SM,Pietrak B,Schwartz B,Blum CA,Disch JS,Caldwell R,Szczepankiewicz B,Oalmann C,Yee Ng P,White BH,Casaubon R,Narayan R,Koppetsch K,Bourbdoi
10.1038/ncomms8645subject
Has Abstractpub_date
2015-07-02 00:00:00pages
7645issn
2041-1723pii
ncomms8645journal_volume
6pub_type
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