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 |
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Pages (from-to) | 716–718 |
Journal | Nature Structural and Molecular Biology |
Volume | 19 |
Issue number | 7 |
DOIs | |
Publication status | Published - Jul 2012 |