Article
An alternative conformation of human TrpRS suggests a role of zinc in activating non-enzymatic function.
RNA biology - 1 Jan 2018
Xu Xiaoling, Zhou Huihao, Zhou Quansheng, Hong Fei, Vo My-Nuong, Niu Wanqiang, Wang Zhiguo, Xiong Xiaolin, Nakamura Kanaha, Wakasugi Keisuke, Schimmel Paul, Yang Xiang-Lei
Abstract excerpt
Tryptophanyl-tRNA synthetase (TrpRS) in vertebrates contains a N-terminal extension in front of the catalytic core. Proteolytic removal of the N-terminal 93 amino acids gives rise to T2-TrpRS, which has potent anti-angiogenic activity mediated through its extracellular interaction with VE-cadherin. Zinc has been shown to have anti-angiogenic effects and can bind to human TrpRS. However, the connection between...
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