Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Cover Figure

ONLINE COVER This week kicks off a series about the structural biology of signaling molecules and complexes. The structural analysis in the Research Article by Lin et al. helped to uncover how ATP and ATP-competitive inhibitors stabilize a conformation of the kinase Akt in which the phosphorylated activating residues are inaccessible to phosphatases. The accompanying Perspective by Humphrey and James discusses the implications of these findings for the regulation of Akt activity. The image shows Akt1 bound to the ATP-competitive inhibitor GDC-0068. [Image: Chris Bickel/AAAS]

[Table of Contents]

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882