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Structure paper

TitleStructural basis for allosteric, substrate-dependent stimulation of SIRT1 activity by resveratrol
Journal, issue, pagesGenes Dev., Vol. 29, Page 1316-1325, Year 2015
Publish dateJun 3, 2015 (structure data deposition date)
AuthorsCao, D. / Wang, M. / Qiu, X. / Liu, D. / Jiang, H. / Yang, N. / Xu, R.M.
External linksGenes Dev. / PubMed:26109052
MethodsX-ray diffraction
Resolution3.2 Å
Structure data

PDB-5btr:
Crystal structure of SIRT1 in complex with resveratrol and an AMC-containing peptide
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-STL:
RESVERATROL

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • synthetic (others)
KeywordsHYDROLASE/SUBSTRATE / Deacetylase / Human Sirtuin 1 / N-terminal domain / Catalytic domain / C-terminal domain / Resveratrol / Substrate / HYDROLASE-SUBSTRATE complex

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