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The Role of Phe82 and Phe351 in Auxin-Induced Substrate Perception by TIR1 Ubiquitin Ligase: A Novel Insight from Molecular Dynamics Simulations

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成果类型:
期刊论文
作者:
Hao, Ge-Fei*;Yang, Guang-Fu(杨光富
通讯作者:
Hao, Ge-Fei
作者机构:
[Yang, Guang-Fu; Hao, Ge-Fei] Cent China Normal Univ, Coll Chem, Minist Educ, Key Lab Pesticide & Chem Biol, Wuhan, Peoples R China.
通讯机构:
[Hao, Ge-Fei] C
Cent China Normal Univ, Coll Chem, Minist Educ, Key Lab Pesticide & Chem Biol, Wuhan, Peoples R China.
语种:
英文
关键词:
Auxins;Hydrogen bonding;Free energy;Crystal structure;Molecular dynamics;Membrane proteins;Solvation;Simulation and modeling
期刊:
PLOS ONE
ISSN:
1932-6203
年:
2010
卷:
5
期:
5
页码:
e10742
基金类别:
National Basic Research Program of ChinaNational Basic Research Program of China [2010CB126103]; NSFCNational Natural Science Foundation of China (NSFC) [20925206, 20932005]
机构署名:
本校为第一且通讯机构
院系归属:
化学学院
摘要:
It is well known that Auxin plays a key role in controlling many aspects of plant growth and development. Crystal structures of Transport inhibitor response 1 (TIR1), a true receptor of auxin, were very recently determined for TIR1 alone and in complexes with auxin and different synthetic analogues and an Auxin/Indole-3-Acetic Acid (Aux/IAA) substrate peptide. However, the dynamic conformational changes of the key residues of TIR1 that take place during the auxin and substrate perception by TIR1 and the detailed mechanism of these changes are s...

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