1Nikolai P. Skiba and Heidi E. Hamm are at the Northwestern University Institute for Neuroscience, Department of Molecular Pharmacology and Biological Chemistry, Northwestern University Medical School, 5-555 Searle, 320 E. Superior, Chicago, Illinois 60611, USA.
2email: h-hamm@nwu.edu
The crystal structure of the catalytic domain of adenylyl cyclase in complex with its activator Gs suggests a surprising allosteric mechanism of activation by formation of a new catalytic site at the interface between conserved dimers of the soluble adenylyl cyclase domains.
activates adenylyl cyclase
suggests a surprising allosteric mechanism of activation by formation of a new catalytic site at the interface between conserved dimers of the soluble adenylyl cyclase domains.
