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

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

Author information

1
MOE Key Laboratory of Protein Sciences, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, China.

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.

PMID:
22659875
DOI:
10.1038/nsmb.2319
[Indexed for MEDLINE]

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