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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
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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.



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