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TitleThe 2.5 angstrom crystal structure of the SIRT1 catalytic domain bound to nicotinamide adenine dinucleotide (NAD+) and an indole (EX527 analogue) reveals a novel mechanism of histone deacetylase inhibition.
Journal, issue, pagesJ. Med. Chem., Vol. 56, Page 963-969, Year 2013
Publish dateNov 28, 2012 (structure data deposition date)
AuthorsZhao, X. / Allison, D. / Condon, B. / Zhang, F. / Gheyi, T. / Zhang, A. / Ashok, S. / Russell, M. / MacEwan, I. / Qian, Y. ...Zhao, X. / Allison, D. / Condon, B. / Zhang, F. / Gheyi, T. / Zhang, A. / Ashok, S. / Russell, M. / MacEwan, I. / Qian, Y. / Jamison, J.A. / Luz, J.G.
External linksJ. Med. Chem. / PubMed:23311358
MethodsX-ray diffraction
Resolution2.5 Å
Structure data

PDB-4i5i:
Crystal structure of the SIRT1 catalytic domain bound to NAD and an EX527 analog
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-4I5:
(6S)-2-chloro-5,6,7,8,9,10-hexahydrocyclohepta[b]indole-6-carboxamide

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / Rossmann Fold / histone deacetylase / epigenetics / cancer / sirtuin / acetylated lysine of histone

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