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The recently determined crystal structure of G sα bound to a catalytically active form of adenylyl cyclase reveals the location of the enzyme's active site and provides the first view of heterotrimeric G protein α subunit activating a downstream effector. Comparison with the structure of a catalytically inactive form of adenylyl cyclase suggests a plausible allosteric mechanism whereby the synergistic activators G sα and forskolin stimulate the activity of adenylyl cyclase.
Program in Molecular Medicine, University of Massachusetts Medical Center, 373 Plantation Street, Worcester, MA 01605, USA E-mail: David.Lambright@ummed.edu