Crystal structures of the human RNA demethylase alkbh5 reveal basis for substrate recognition

Chong Feng; Yang Liu; Guoqiang Wang; Zengqin Deng; Qi Zhang; Wei Wu; Yufeng Tong; Changmei Cheng; Zhongzhou Chen

doi:10.1074/jbc.M113.546168

Crystal structures of the human RNA demethylase alkbh5 reveal basis for substrate recognition

Chong Feng, Yang Liu, Guoqiang Wang, Zengqin Deng, Qi Zhang, Wei Wu, Yufeng Tong, Changmei Cheng, Zhongzhou Chen

Department of Cell Biology & Physiology

Research output: Contribution to journal › Article › peer-review

124 Scopus citations

Abstract

Background: Human AlkB homolog 5 (Alkbh5) is an RNA demethylase that erases m6A modification., Results: Crystal structures of an enzymatically active Alkbh5 construct in complex with cofactors or small molecules were determined., Conclusion: Structure and activity analyses showed that Alkbh5 strongly prefers single-stranded oligos and small molecule inhibitors., Significance: The Alkbh5 structure reveals potential for structure-based design of selective inhibitors.

Original language	English
Pages (from-to)	11571-11583
Number of pages	13
Journal	Journal of Biological Chemistry
Volume	289
Issue number	17
DOIs	https://doi.org/10.1074/jbc.M113.546168
State	Published - Apr 25 2014

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title = "Crystal structures of the human RNA demethylase alkbh5 reveal basis for substrate recognition",

abstract = "Background: Human AlkB homolog 5 (Alkbh5) is an RNA demethylase that erases m6A modification., Results: Crystal structures of an enzymatically active Alkbh5 construct in complex with cofactors or small molecules were determined., Conclusion: Structure and activity analyses showed that Alkbh5 strongly prefers single-stranded oligos and small molecule inhibitors., Significance: The Alkbh5 structure reveals potential for structure-based design of selective inhibitors.",

author = "Chong Feng and Yang Liu and Guoqiang Wang and Zengqin Deng and Qi Zhang and Wei Wu and Yufeng Tong and Changmei Cheng and Zhongzhou Chen",

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T1 - Crystal structures of the human RNA demethylase alkbh5 reveal basis for substrate recognition

AU - Feng, Chong

AU - Liu, Yang

AU - Wang, Guoqiang

AU - Deng, Zengqin

AU - Zhang, Qi

AU - Wu, Wei

AU - Tong, Yufeng

AU - Cheng, Changmei

AU - Chen, Zhongzhou

PY - 2014/4/25

Y1 - 2014/4/25

N2 - Background: Human AlkB homolog 5 (Alkbh5) is an RNA demethylase that erases m6A modification., Results: Crystal structures of an enzymatically active Alkbh5 construct in complex with cofactors or small molecules were determined., Conclusion: Structure and activity analyses showed that Alkbh5 strongly prefers single-stranded oligos and small molecule inhibitors., Significance: The Alkbh5 structure reveals potential for structure-based design of selective inhibitors.

AB - Background: Human AlkB homolog 5 (Alkbh5) is an RNA demethylase that erases m6A modification., Results: Crystal structures of an enzymatically active Alkbh5 construct in complex with cofactors or small molecules were determined., Conclusion: Structure and activity analyses showed that Alkbh5 strongly prefers single-stranded oligos and small molecule inhibitors., Significance: The Alkbh5 structure reveals potential for structure-based design of selective inhibitors.

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U2 - 10.1074/jbc.M113.546168

DO - 10.1074/jbc.M113.546168

M3 - Article

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AN - SCOPUS:84899425559

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VL - 289

SP - 11571

EP - 11583

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 17

ER -

Crystal structures of the human RNA demethylase alkbh5 reveal basis for substrate recognition

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