Abstract
Analysis of cyclic nucleotide binding (CNB) domains shows that they have evolved to sense a wide variety of second messenger signals; a mechanism for allosteric regulation by CNB domains is proposed.
Highlights
The cyclic nucleotide binding (CNB) domain regulates signaling pathways in both eukaryotes and prokaryotes
Because these functional domains play an important role in CNB domain functions, they were used as markers for annotation and classification
The co-occurrence of kinases, phosphatase and CNB domains in the same operon is interesting because previous bioinformatics analysis had failed to provide any evidence for a cAMP or cGMP dependent regulation of kinase activity in plants [21]
Summary
The cyclic nucleotide binding (CNB) domain regulates signaling pathways in both eukaryotes and prokaryotes. The first characterized family containing a CNB domain in prokaryotes is the CAP (catabolite gene activator protein) family of transcriptional regulators [7] that contain a DNA binding helix-turnhelix (HTH) domain covalently linked to the CNB domain [8]. This domain organization is important for CAP function as it couples cAMP binding functions of the CNB domain with DNA binding functions of the HTH domain [9]. The CprK subfamily of transcriptional regulators binds to ortho-chlorophenolic compounds in the cAMP binding pocket [12]
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