Solving AMPK

The enzyme AMP-activated protein kinase (AMPK) has been shown to be central to regulating several metabolic systems such as glucose uptake, oxidation of fatty acids, and insulin sensitivity, but the crystal structure of the mammalian enzyme remained elusive.ﾠBing Xiao and others from the United Kingdom's National Institute for Medical Research used X-ray crystallography to map the structure of AMPK when bound to AMP and ATP, which the enzyme binds competitively,1 illuminating AMPK regulation.


	The article you are attempting to read is Premium content which is only available to our online subscribers.

Subscribing to The Scientist is easy and inexpensive.

And you can choose from many options. Try us out with an online day pass starting at only $4.95. Or, get it all with unlimited online access to The Scientist Archive and door-to-door delivery of our monthly print magazine.


	The Scientist also offers site licenses to institutions and organizations. When your librarian adds The Scientist to the library's collection, you can get unlimited online access through your place of work or study. Recommend The Scientist today