Tetrathiomolybdate induces dimerization of the metal-binding domain of ATPase and inhibits platination of the protein

Tetrathiomolybdate induces dimerization of the metal-binding domain of ATPase and inhibits platination of the protein

Tetrathiomolybdate (TM) and Cu-ATPases, e.g. Wilson (WLN) protein, affect the efficacy of common anticancer drug cisplatin. Here, the authors show that TM generates a protein dimer with a WLN domain by expelling copper and provide insight into the synergy of TM and cisplatin in cancer chemotherapy.

Bibliographic Details
Main Authors: Tiantian Fang, Wanbiao Chen, Yaping Sheng, Siming Yuan, Qiaowei Tang, Gongyu Li, Guangming Huang, Jihu Su, Xuan Zhang, Jianye Zang, Yangzhong Liu
Format: Article
Language:English
Published: Nature Publishing Group 2019-01-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-018-08102-z

Internet

https://doi.org/10.1038/s41467-018-08102-z

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