Structural basis for AMP binding to mammalian AMP-activated protein kinase

Bing Xiao, Richard Heath, Peter Saiu, Fiona C. Leiper, Philippe Leone, Chun Jing, Philip A. Walker, Lesley Haire, John F. Eccleston, Colin T. Davis, Stephen R. Martin (), David Carling () and Steven J. Gamblin ()
Additional contact information
Bing Xiao: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Richard Heath: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Peter Saiu: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Fiona C. Leiper: MRC Clinical Sciences Centre, Hammersmith Hospital Campus, Imperial College, DuCane Road, London W12 0NN, UK
Philippe Leone: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Chun Jing: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Philip A. Walker: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Lesley Haire: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
John F. Eccleston: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Colin T. Davis: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
Stephen R. Martin: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
David Carling: MRC Clinical Sciences Centre, Hammersmith Hospital Campus, Imperial College, DuCane Road, London W12 0NN, UK
Steven J. Gamblin: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK

Nature, 2007, vol. 449, issue 7161, 496-500

Abstract: AMP-activated protein kinase (AMPK) is a central regulator of energy homeostasis in mammals. This crystal structure of the trimeric regulatory fragment of mammalian AMPK reveals the modes of AMP and ATP binding.

Date: 2007
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DOI: 10.1038/nature06161

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