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

关键词：

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学科分类号：

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.

引用

页码：1304 / 1309

页数：5

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