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PROSITE documentation PDOC00691 [for PROSITE entry PS00888] |
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. Such a domain is known to exist in the following proteins:
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. We developed two signature patterns for this domain. The first pattern is located within β-barrels 2 and 3 and contains the first two conserved Gly. The second pattern is located within β-barrels 6 and 7 and contains the third conserved Gly as well as the three other invariant residues.
Last update:December 2004 / Pattern and text revised.
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PROSITE methods (with tools and information) covered by this documentation:
1 | Authors | Weber I.T. Shabb J.B. Corbin J.D. |
Title | Predicted structures of the cGMP binding domains of the cGMP-dependent protein kinase: a key alanine/threonine difference in evolutionary divergence of cAMP and cGMP binding sites. | |
Source | Biochemistry 28:6122-6127(1989). | |
PubMed ID | 2550070 |
2 | Authors | Kaupp U.B. |
Title | The cyclic nucleotide-gated channels of vertebrate photoreceptors and olfactory epithelium. | |
Source | Trends Neurosci. 14:150-157(1991). | |
PubMed ID | 1710853 |
3 | Authors | Shabb J.B. Corbin J.D. |
Title | Cyclic nucleotide-binding domains in proteins having diverse functions. | |
Source | J. Biol. Chem. 267:5723-5726(1992). | |
PubMed ID | 1313416 |