D
IPR000595

Cyclic nucleotide-binding domain

InterPro entry
Short namecNMP-bd_dom
Overlapping
homologous
superfamilies
 

Description

Proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues
[1, 2, 3]
. The best studied of these proteins is the prokaryotic catabolite gene activator (also known as the cAMP receptor protein) (gene crp) where such a domain is known to be composed of three α-helices and a distinctive eight-stranded, antiparallel β-barrel structure. There are six invariant amino acids in this domain, three of which are glycine residues that are thought to be essential for maintenance of the structural integrity of the β-barrel. cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain. The cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain. The cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section. Vertebrate cyclic nucleotide-gated ion-channels also contain this domain. Two such cations channels have been fully characterised, one is found in rod cells where it plays a role in visual signal transduction.

References

1.Phylogeny of the bacterial superfamily of Crp-Fnr transcription regulators: exploiting the metabolic spectrum by controlling alternative gene programs. Korner H, Sofia HJ, Zumft WG. FEMS Microbiol. Rev. 27, 559-92, (2003). View articlePMID: 14638413

2.Transcription activation by catabolite activator protein (CAP). Busby S, Ebright RH. J. Mol. Biol. 293, 199-213, (1999). View articlePMID: 10550204

3.The cyclic nucleotide-gated channels of vertebrate photoreceptors and olfactory epithelium. Kaupp UB. Trends Neurosci. 14, 150-7, (1991). View articlePMID: 1710853

Cross References

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