Gs alpha meets its target--shedding light on a key signal transduction event.
The recently determined crystal structure of Gs alpha 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 alpha 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 Gs alpha and forskolin stimulate the activity of adenylyl cyclase.
Dumas
J J
JJ
Program in Molecular Medicine, University of Massachusetts Medical Center, 373 Plantation Street, Worcester, MA 01605, USA.
Lambright
D G
DG
D000255:Adenosine Triphosphate / Q000737:chemistry; D000262:Adenylyl Cyclases / Q000737:chemistry*; D000494:Allosteric Regulation / Q000502:physiology; D001665:Binding Sites / Q000502:physiology; D019205:GTP-Binding Protein alpha Subunits, Gs / Q000737:chemistry*; D006160:Guanosine Triphosphate / Q000737:chemistry; D008958:Models, Molecular; D011487:Protein Conformation; D015398:Signal Transduction / Q000502:physiology*
D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate; D019205:GTP-Binding Protein alpha Subunits, Gs; D000262:Adenylyl Cyclases