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- W2485553437 abstract "This chapter focuses on the atomic structures of cGMP- or cAMP-binding GAF domains from the PDEs and adenylyl cyclases. These include the X-ray crystal structures of the regulatory segments, consisting of tandem GAF domains, from the mammalian phosphodiesterase PDE2A, and from a cyanobacterial adenylyl cyclase. cAMP and cGMP are important second messengers in cells. Their levels are controlled by activities of adenylyl and guanylyl cyclases (AC or GC), the enzymes that catalyze their synthesis, and cyclic nucleotide phosphodiesterases (PDEs), which hydrolyze these 3′,5′ cyclic nucleotides to their inactive 5′-nucleotide monophosphates. Of the 11 PDE families identified in mammalian tissues, all contain an N-terminal regulatory segment and a C-terminal catalytic domain. The first crystal structures of cyclic nucleotide-binding GAF domains have answered several basic questions about the mode of ligand binding and dimerization, but have also raised many others. A putative GAF ligand was found when the cAMP-stimulated cyanobacterial adenylyl cyclase cyaB1 was shown to be negatively regulated through its GAF domains by Na+, with an IC50 of 14.3 mM. Ultimately, crystal or NMR structures will be needed for the various PDE domains with and without bound ligands to visualize the conformational changes that occur upon binding. Structures of the full-length holoenzymes may also be required to visualize the allosteric mechanism. Since these small molecule binding GAF domains are intimately involved in regulation of so many different enzymes, they are also likely to become good targets for drug development." @default.
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- W2485553437 date "2010-01-01" @default.
- W2485553437 modified "2023-09-23" @default.
- W2485553437 title "Cyclic Nucleotide-Binding GAF Domains in Phosphodiesterases and Adenylyl Cyclases" @default.
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- W2485553437 doi "https://doi.org/10.1016/b978-0-12-374145-5.00187-x" @default.
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