AMP-activated protein kinase undergoes nucleotide-dependent conformational changes

Lei Chen; Jue Wang; Yuan-Yuan Zhang; S. Frank Yan; Dietbert Neumann; Uwe Schlattner; Zhi-Xin Wang; Jia-Wei Wu

doi:10.1038/nsmb.2319

AMP-activated protein kinase undergoes nucleotide-dependent conformational changes

Lei Chen
, Jue Wang
, Yuan-Yuan Zhang
, S. Frank Yan
, Dietbert Neumann
, Uwe Schlattner
, Zhi-Xin Wang
, Jia-Wei Wu^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

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.

Original language	English
Pages (from-to)	716–718
Number of pages	3
Journal	Nature Structural and Molecular Biology
Volume	19
Issue number	7
DOIs	https://doi.org/10.1038/nsmb.2319
Publication status	Published - Jul 2012

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10.1038/nsmb.2319

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title = "AMP-activated protein kinase undergoes nucleotide-dependent conformational changes",

abstract = "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.",

author = "Lei Chen and Jue Wang and Yuan-Yuan Zhang and Yan, \{S. Frank\} and Dietbert Neumann and Uwe Schlattner and Zhi-Xin Wang and Jia-Wei Wu",

year = "2012",

month = jul,

doi = "10.1038/nsmb.2319",

language = "English",

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journal = "Nature Structural and Molecular Biology",

issn = "1545-9993",

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T1 - AMP-activated protein kinase undergoes nucleotide-dependent conformational changes

AU - Chen, Lei

AU - Wang, Jue

AU - Zhang, Yuan-Yuan

AU - Yan, S. Frank

AU - Neumann, Dietbert

AU - Schlattner, Uwe

AU - Wang, Zhi-Xin

AU - Wu, Jia-Wei

PY - 2012/7

Y1 - 2012/7

N2 - 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.

AB - 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.

U2 - 10.1038/nsmb.2319

DO - 10.1038/nsmb.2319

M3 - Article

C2 - 22659875

SN - 1545-9993

VL - 19

SP - 716

EP - 718

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

IS - 7

ER -

AMP-activated protein kinase undergoes nucleotide-dependent conformational changes

Abstract

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