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• W2149871191 abstract "Cyclic nucleotide phosphodiesterases (PDEs) regulate all pathways that use cGMP or cAMP as a second messenger. Five of the 11 PDE families have regulatory segments containing GAF domains, 3 of which are known to bind cGMP. In PDE2 binding of cGMP to the GAF domain causes an activation of the catalytic activity by a mechanism that apparently is shared even in the adenylyl cyclase of Anabaena, an organism separated from mouse by 2 billion years of evolution. The 2.9-Å crystal structure of the mouse PDE2A regulatory segment reported in this paper reveals that the GAF A domain functions as a dimerization locus. The GAF B domain shows a deeply buried cGMP displaying a new cGMP-binding motif and is the first atomic structure of a physiological cGMP receptor with bound cGMP. Moreover, this cGMP site is located well away from the region predicted by previous mutagenesis and structural genomic approaches." @default.
• W2149871191 created "2016-06-24" @default.
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• W2149871191 date "2002-09-23" @default.
• W2149871191 modified "2023-09-25" @default.
• W2149871191 title "The two GAF domains in phosphodiesterase 2A have distinct roles in dimerization and in cGMP binding" @default.
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• W2149871191 doi "https://doi.org/10.1073/pnas.192374899" @default.
• W2149871191 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/130621" @default.
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