Crystal structure of the heterotrimer core of Saccharomyces cerevisiae AMPK homologue SNF1

Gabriele A. Amodeo, Michael J. Rudolph and Liang Tong ()
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Gabriele A. Amodeo: Columbia University, New York, New York 10027, USA
Michael J. Rudolph: Columbia University, New York, New York 10027, USA
Liang Tong: Columbia University, New York, New York 10027, USA

Nature, 2007, vol. 449, issue 7161, 492-495

Abstract: AMP-activated protein kinase is a central regulator of energy homeostasis in mammals, and the Saccharomyces cerevisiae homologue SNF1 is essential for responses to nutrient starvation. This structure reveals features such as the ligand-binding site in the γ-subunit, the carbohydrate-binding domain in the β-subunit and a regulatory sequence in the α-subunit.

Date: 2007
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DOI: 10.1038/nature06127

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