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. 2012 Jun 3;19(7):716-8.
doi: 10.1038/nsmb.2319.

AMP-activated protein kinase undergoes nucleotide-dependent conformational changes

Lei Chen  1 , Jue Wang, Yuan-Yuan Zhang, S Frank Yan, Dietbert Neumann, Uwe Schlattner, Zhi-Xin Wang, Jia-Wei Wu
Affiliations

AMP-activated protein kinase undergoes nucleotide-dependent conformational changes

Lei Chen et al. Nat Struct Mol Biol. .

Abstract

The energy sensor AMP-activated protein kinase (AMPK) is a heterotrimeric complex that is allosterically activated by AMP binding to the γ subunit. Cocrystal structures of the mammalian AMPK core reveal occlusion of nucleotide-binding site 3 of the γ 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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