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Insights into 4-hydroxyphenylpyruvate dioxygenase-inhibitor interactions from comparative structural biology

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成果类型:
期刊论文
作者:
Lin, Hong-Yan;Dong, Jin;Dong, Jiangqing;Yang, Wen-Chao;Yang, Guang-Fu
通讯作者:
Yang, GF
作者机构:
[Yang, Guang-Fu; Yang, Wen-Chao; Yang, GF; Dong, Jin; Lin, Hong-Yan; Dong, Jiangqing] Cent China Normal Univ, Int Joint Res Ctr Intelligent Biosensor Technol &, Natl Key Lab Green Pesticide, Key Lab Pesticide & Chem Biol,Minist Educ, Wuhan 430079, Peoples R China.
[Dong, Jiangqing] Chime Biol Ltd, 388 Gaoxin Rd, Wuhan, Peoples R China.
通讯机构:
[Yang, GF ] C
Cent China Normal Univ, Int Joint Res Ctr Intelligent Biosensor Technol &, Natl Key Lab Green Pesticide, Key Lab Pesticide & Chem Biol,Minist Educ, Wuhan 430079, Peoples R China.
语种:
英文
关键词:
4-hydroxyphenylpyruvate dioxygenase;crystal structure;inhibitor;slow-binding kinetics
期刊:
Trends in Biochemical Sciences
ISSN:
0968-0004
年:
2023
卷:
48
期:
6
页码:
568-584
基金类别:
National Key Research and Development Program, China [2021YFD1700100]; National Natural Science Foundation, China [21837001, 22007035]; Key Research and Development Program, Hubei Province, China [2022BBA001]; Fundamental Research Funds for the Central Universities, China
机构署名:
本校为第一且通讯机构
院系归属:
化学学院
摘要:
4-Hydroxyphenylpyruvate dioxygenase (HPPD) plays a key role in tyrosine metabolism and has been identified as a promising target for herbicide and drug discovery. The structures of HPPD complexed with different types of inhibitors have been determined previously. We summarize the structures of HPPD complexed with structurally diverse molecules, including inhibitors, natural products, substrates, and catalytic intermediates; from these structures, the detailed inhibitory mechanisms of different inhibitors were analyzed and compared, and the key structural factors determining the slow-binding be...

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