+Search query
-Structure paper
Title | The 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, pages | J. Med. Chem., Vol. 56, Page 963-969, Year 2013 |
Publish date | Nov 28, 2012 (structure data deposition date) |
Authors | Zhao, 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 links | J. Med. Chem. / PubMed:23311358 |
Methods | X-ray diffraction |
Resolution | 2.5 Å |
Structure data | PDB-4i5i: |
Chemicals | ChemComp-4I5: ChemComp-NAD: ChemComp-ZN: ChemComp-HOH: |
Source |
|
Keywords | HYDROLASE / Rossmann Fold / histone deacetylase / epigenetics / cancer / sirtuin / acetylated lysine of histone |