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PDBsum entry 4eal
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References listed in PDB file
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Key reference
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Title
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Amp-Activated protein kinase undergoes nucleotide-Dependent conformational changes.
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Authors
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L.Chen,
J.Wang,
Y.Y.Zhang,
S.F.Yan,
D.Neumann,
U.Schlattner,
Z.X.Wang,
J.W.Wu.
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Ref.
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Nat Struct Biol, 2012,
19,
716-718.
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PubMed id
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Abstract
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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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