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Interactions of aryloxyphenoxypropionic acids with sensitive and resistant acetyl-coenzyme A carboxylase by homology modeling and molecular dynamic simulations

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成果类型:
期刊论文、会议论文
作者:
Zhu, Xiao-Lei;Zhang, Li;Chen, Qiong;Wan, Jian;Yang, Guang-Fu*杨光富
通讯作者:
Yang, Guang-Fu
作者机构:
[Yang, Guang-Fu; Zhu, Xiao-Lei; Chen, Qiong; Zhang, Li; Wan, Jian; Yang, GF] Cent China Normal Univ, Coll Chem, Minist Educ, Key Lab Pesticide & Chem Biol, Wuhan 430079, Peoples R China.
通讯机构:
[Yang, Guang-Fu] C
Cent China Normal Univ, Coll Chem, Minist Educ, Key Lab Pesticide & Chem Biol, Wuhan 430079, Peoples R China.
语种:
英文
期刊:
Journal of Chemical Information and Modeling
ISSN:
1549-9596
年:
2006
卷:
46
期:
4
页码:
1819-1826
会议名称:
The 3rd International Conference of Molecular Simulations and Applied Informatics Technologies(第三届国际分子模拟与信息技术应用学术会议)
会议论文集名称:
第三届国际分子模拟与信息技术应用学术会议
会议时间:
2007-04-01
会议地点:
杭州
会议赞助商:
中国化学会<&wdkj&>浙江工业大学
机构署名:
本校为第一且通讯机构
院系归属:
化学学院
摘要:
Acetyl-coenzyme A carboxylase (ACCase) has been identified as one of the most important targets of herbicides. In the present study, we constructed homology models of the carboxyl-transferase (CT) domain of ACCase from sensitive and resistant foxtail and used these models as templates to study the molecular mechanism of herbicide resistance and stereochemistry-activity relationships of aryloxyphenoxypropionates (APPs). In the homology modeling structures, the dimer of the CT domain was formed by the side-to-side arrangement of the two monomers, in such a way that the N domain of one molecule i...

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