A crystallized view of AMPK activation

Lawrence H Young

doi:10.1016/j.cmet.2009.06.008

A crystallized view of AMPK activation

Cell Metab. 2009 Jul;10(1):5-6. doi: 10.1016/j.cmet.2009.06.008.

Author

Lawrence H Young¹

Affiliation

¹ Section of Cardiovascular Medicine, Departments of Internal Medicine and Physiology, Yale University School of Medicine, New Haven, CT 06520, USA. lawrence.young@yale.edu

PMID: 19583947
DOI: 10.1016/j.cmet.2009.06.008

Abstract

AMP-activated protein kinase (AMPK) is a key metabolic regulator. Recent work (Chen et al., 2009) elucidates the structural interaction between the autoinhibitory sequence and the kinase domain of the AMPK catalytic subunit. Enhanced understanding of the molecular mechanics of AMPK activation might lead to novel therapeutic approaches.

MeSH terms

AMP-Activated Protein Kinases / chemistry
AMP-Activated Protein Kinases / metabolism*
Adenosine Monophosphate / metabolism
Binding Sites
Enzyme Activation
Protein Structure, Tertiary

Substances

Adenosine Monophosphate
AMP-Activated Protein Kinases