Mechanism of allosteric activation of SAMHD1 by dGTP

被引：0
|
作者：
Xiaoyun Ji
Ying Wu
Junpeng Yan
Jennifer Mehrens
Haitao Yang
Maria DeLucia
Caili Hao
Angela M Gronenborn
Jacek Skowronski
Jinwoo Ahn
Yong Xiong
机构：
[1] Yale University,Department of Molecular Biophysics and Biochemistry
[2] University of Pittsburgh School of Medicine,Department of Structural Biology
[3] Pittsburgh Center for HIV Protein Interactions,Department of Molecular Biology and Microbiology
[4] University of Pittsburgh School of Medicine,undefined
[5] Case Western Reserve School of Medicine,undefined
[6] Present address: School of Life Sciences,undefined
[7] Tianjin University,undefined
[8] Tianjin,undefined
[9] China.,undefined
来源：
Nature Structural & Molecular Biology | 2013年 / 20卷
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摘要：
The dNTPase SAMHD1 inhibits infection by HIV-1 and other retroviruses. In the presence of dGTP, the enzyme forms tetramers and becomes active, a process that is now elucidated by structural, biochemical and cellular analyses of human SAMHD1. Binding of dGTP to four allosteric sites promotes tetramerization and induces a conformational change in the substrate-binding pocket to activate the enzyme.
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页码：1304 / 1309
页数：5
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