Structure of the adenylyl cyclase catalytic core

@article{Zhang1997StructureOT,
  title={Structure of the adenylyl cyclase catalytic core},
  author={Gongyi Zhang and Yu Liu and Arnold E Ruoho and James H. Hurley},
  journal={Nature},
  year={1997},
  volume={386},
  pages={247-253}
}
Mammalian adenylyl cyclases contain two conserved regions, C1 and C2, which are responsible for forskolin- and G-protein-stimulated catalysis. The structure of the C2 catalytic region of type II rat adenylyl cyclase has an α/β class fold in a wreath-like dimer, which has a central cleft. Two forskolin molecules bind in hydrophobic pockets at the ends of cleft. The central part of the cleft is lined by charged residues implicated in ATP binding. Forskolin appears to activate adenylyl cyclase by… 
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TLDR
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TLDR
It is demonstrated that myristoylated guanosine 5′-3-O-(thio)triphosphate-Giα1 forms a stable complex with the C1 (but not the C2) domain of type V adenylyl cyclase, suggesting bidirectional regulation of activity by homologous G protein α subunits.
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