Mechanism of allosteric activation of SIRT6 revealed by the action of rationally designed activators.
10.1016/j.apsb.2020.09.010
- Author:
Shaoyong LU
1
;
Yingyi CHEN
1
;
Jiacheng WEI
1
;
Mingzhu ZHAO
2
;
Duan NI
3
;
Xinheng HE
1
;
Jian ZHANG
1
Author Information
1. Department of Pathophysiology, Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Shanghai Jiao Tong University, School of Medicine, Shanghai 200025, China.
2. State Key Laboratory of Oncogenes and Related Genes, Renji Hospital, Shanghai Jiao Tong University, School of Medicine, Shanghai 200127, China.
3. The Charles Perkins Centre, University of Sydney, Sydney NSW 2006, Australia.
- Publication Type:Journal Article
- Keywords:
ADPR, ADP-ribose;
Allosteric driver;
Allosteric mechanisms;
Allosteric sites;
Drug design;
EC50, Effective concentration;
Enzyme catalysis;
FDL, Fluor de Lys;
H3K56, histone 3 lysine 56;
H3K9, histone 3 lysine 9;
HPLC, high-performance liquid chromatography;
MD, molecular dynamics;
MST, microscale thermophoresis;
Myr-H3K9, myristoyl H3K9;
NAM, nicotinamide;
PCA, principal component analysis;
Protein dynamics;
RMSD, root-mean-square deviation;
SIRT6, sirtuin 6
- From:
Acta Pharmaceutica Sinica B
2021;11(5):1355-1361
- CountryChina
- Language:English
-
Abstract:
The recent discovery of activator compounds binding to an allosteric site on the NAD
