AMP-activated protein kinase undergoes nucleotide-dependent conformational changes.
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.
MOE Key Laboratory of Protein Sciences, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, China.
Lei
L
Chen
Jue
J
Wang
Yuan-Yuan
YY
Zhang
S Frank
SF
Yan
Dietbert
D
Neumann
Uwe
U
Schlattner
Zhi-Xin
ZX
Wang
Jia-Wei
JW
Wu
D055372:AMP-Activated Protein Kinases / Q000737:chemistry / Q000378:metabolism*; D000227:Adenine Nucleotides / Q000378:metabolism*; D000494:Allosteric Regulation; D011487:Protein Conformation
D000227:Adenine Nucleotides; D055372:AMP-Activated Protein Kinases