The recently determined crystal structure of G(s alpha) bound to a cat
alytically active form of adenylyl cyclase reveals the location of the
enzyme's active site and provides the first view of heterotrimeric G
protein alpha subunit activating a downstream effector, Comparison wit
h the structure of a catalytically inactive form of adenylyl cyclase s
uggests a plausible allosteric mechanism whereby the synergistic activ
ators G(s alpha) and forskolin stimulate the activity of adenylyl cycl
ase, (C) Current Biology Ltd ISSN 0969-2126.