AMP-activated protein kinase undergoes nucleotide-dependent conformational changes

被引：106

作者：

Chen, Lei ^{[1
]}

Wang, Jue ^{[1
]}

Zhang, Yuan-Yuan ^{[1
]}

Yan, S. Frank ^{[2
]}

Neumann, Dietbert ^{[3
]}

Schlattner, Uwe ^{[4
,5
]}

Wang, Zhi-Xin ^{[1
]}

Wu, Jia-Wei ^{[1
]}

机构：

[1] Tsinghua Univ, Sch Life Sci, MOE Key Lab Prot Sci, Tsinghua Peking Ctr Life Sci, Beijing 100084, Peoples R China

[2] Roche Pharma Res & Early Dev, Mol Design & Biostruct, Shanghai, Peoples R China

[3] Maastricht Univ, Cardiovasc Res Inst, Maastricht, Netherlands

[4] Inst Natl Sante & Rech Med, Grenoble, France

[5] Univ Grenoble 1, Lab Fundamental & Appl Bioenerget, Grenoble, France

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2012年 / 19卷 / 07期

关键词：

STRUCTURAL BASIS; BINDING; SITE; ADP;

D O I：

10.1038/nsmb.2319

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

The energy sensor AMP-activated protein kinase (AMPK) is a heterotrimeric complex that is allosterically activated by AMP binding to the gamma subunit. Cocrystal structures of the mammalian AMPK core reveal occlusion of nucleotide-binding site 3 of the gamma subunit in the presence of ATP. However, site 3 is occupied in the presence of AMP. Mutagenesis studies indicate that sites 3 and 4 are important for AMPK allosteric activation.

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页码：716 / +

页数：4

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