Crystallographic and SAR analyses reveal the high requirements needed to selectively and potently inhibit SIRT2 deacetylase and decanoylase.
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ABSTRACT:
SUBMITTER: Yang LL
PROVIDER: S-EPMC6350764 | biostudies-literature | 2019 Jan
REPOSITORIES: biostudies-literature
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Crystallographic and SAR analyses reveal the high requirements needed to selectively and potently inhibit SIRT2 deacetylase and decanoylase.
Yang Ling-Ling LL Xu Wei W Yan Jie J Su Hui-Lin HL Yuan Chen C Li Chao C Zhang Xing X Yu Zhu-Jun ZJ Yan Yu-Hang YH Yu Yamei Y Chen Qiang Q Wang Zhouyu Z Li Lin L Qian Shan S Li Guo-Bo GB
MedChemComm 20181207 1
A high-quality X-ray crystal structure reveals the mechanism of compound <b>1a</b> inhibiting SIRT2 deacetylase and decanoylase. Structure-activity relationship (SAR) analysis of the synthesized derivatives of <b>1a</b> reveals the high requirements needed for selective inhibitors to bind with the induced hydrophobic pocket and potently inhibit sirtuin 2 deacetylase. ...[more]
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