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PDBsum entry 3hyh
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the protein kinase domain of yeast AMP-Activated protein kinase snf1.
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Authors
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M.J.Rudolph,
G.A.Amodeo,
Y.Bai,
L.Tong.
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Ref.
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Biochem Biophys Res Commun, 2005,
337,
1224-1228.
[DOI no: ]
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PubMed id
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Abstract
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AMP-activated protein kinase (AMPK) is a master metabolic regulator, and is an
important target for drug development against diabetes, obesity, and other
diseases. AMPK is a hetero-trimeric enzyme, with a catalytic (alpha) subunit,
and two regulatory (beta and gamma) subunits. Here we report the crystal
structure at 2.2A resolution of the protein kinase domain (KD) of the catalytic
subunit of yeast AMPK (commonly known as SNF1). The Snf1-KD structure shares
strong similarity to other protein kinases, with a small N-terminal lobe and a
large C-terminal lobe. Two negative surface patches in the structure may be
important for the recognition of the substrates of this kinase.
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