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.
Subscribe

Logo for

Science 335 (6072): 1055-1056

Copyright © 2012 by the American Association for the Advancement of Science

Structural Origins of Receptor Bias

Stephen R. Sprang, and Jackson Chief Elk

Center for Biomolecular Structure and Dynamics, University of Montana, Missoula, MT 59812, USA.


Figure 1
View larger version (61K):
[in this window]
[in a new window]

  		Functionally selective. Binding of agonists to the β2AR results in conformational changes that displace TM5 and TM6 (green) and/or TM7 (blue). The conformational changes permit G protein (Gs) binding or receptor phosphorylation (P) and β-arrestin binding. β-arrestin binding blocks G protein signaling. The aromatic moiety of the agonist (isoproterenol shown) contacts TM5 and TM6, whereas the hydroxylamine substituent interacts with TM3 and TM7.

CREDIT: C. BICKEL/SCIENCE

 

To Advertise     Find Products

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