Primary structure of cAMP‐gated channel from bovine olfactory epithelium

Ludwig, Jost; Margalit, Talya; Eismann, Elisabeth; Lancet, Doron; Kaupp, U. Benjamin

doi:10.1016/0014-5793(90)81226-e

Cited by 255 publications

(106 citation statements)

References 23 publications

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“…The putative cyclic-nucleotide-binding domain located in AtCNGC2 has structural features consistent with corresponding domains in animals cng channels (compare with Ludwig et al, 1990;Bonigk et al, 1993). A key amino acid residue associated with nucleotide binding is present as a conservative substitution in AtCNGC2.…”

Section: Resultsmentioning

confidence: 57%

Cloning and First Functional Characterization of a Plant Cyclic Nucleotide-Gated Cation Channel

et al. 1999

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Section: Resultsmentioning

confidence: 57%

Cloning and First Functional Characterization of a Plant Cyclic Nucleotide-Gated Cation Channel

et al. 1999

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“…Among others, the cNMP superfamily includes a variety of bacterial regulators, such as the catabolite gene activator protein (CAP) (Eron et al 1971;Weber and Steitz 1987), cyclic nucleotide-gated ion channels (Nakamura and Gold 1987;Ludwig et al 1990), guanine nucleotide exchange factors (Kawasaki et al 1998), and the regulators of PKA and PKG. The distinctive feature of the members of the superfamily is the presence of a common structural domain of about 120 residues (Shabb and Corbin 1992) capable of binding cyclic nucleotides.…”

Section: Introductionmentioning

confidence: 99%

Classification and Phylogenetic Analysis of the cAMP-Dependent Protein Kinase Regulatory Subunit Family

2002

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Abstract. The members of the PKA regulatory subunit family (PKA-R family) were analyzed by multiple sequence alignment and clustering based on phylogenetic tree construction. According to the phylogenetic trees generated from multiple sequence alignment of the complete sequences, the PKA-R family was divided into four subfamilies (types I to IV). Members of each subfamily were exclusively from animals (types I and II), fungi (type III), and alveolates (type IV). Application of the same methodology to the cAMP-binding domains, and subsequently to the region delimited by ␤-strands 6 and 7 of the crystal structures of bovine RI␣ and rat RII␤ (the phosphate-binding cassette; PBC), proved that this highly conserved region was enough to classify unequivocally the members of the PKA-R family. A single signature sequence, F-G-E-[LIV]-A-L-[LIMV]-x(3)-[PV]-R-[ANQV]-A, corresponding to the PBC was identified which is characteristic of the PKA-R family and is sufficient to distinguish it from other members of the cyclic nucleotide-binding protein superfamily. Specific determinants for the A and B domains of each Rsubunit type were also identified. Conserved residues defining the signature motif are important for interaction with cAMP or for positioning the residues that directly interact with cAMP. Conversely, residues that define subfamilies or domain types are not conserved and are mostly located on the loop that connects ␣-helix BЈ and ␤ strand 7.

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“…The cDNAs encoding the CNG channels involved in visual and olfactory transductions have been cloned from several vertebrate species [10][11][12][13][14][15][16][17][18]. It is now clear that the native channels are composed of at least c~-and [3-subunits.…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning, functional expression and chromosomal localization of a human homolog of the cyclic nucleotide‐gated ion channel of retinal cone photoreceptors

Grunwald

Yau

1996

FEBS Letters

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We have cloned from human retina a cyclic nucleotide-gated (CNG) ion channel that is distinct from the one found in rod photoreceptors. This channel protein is highly homologous to the CNG channel that recently has been cloned from bovine testis and kidney and has been shown to be present in retinal cone photoreceptors. When expressed in human embryonic kidney cells, the protein forms functional ion channels with properties broadly similar to those described for the cloned bovine channel. The gene for this channel resides on chromosome 2.

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Primary structure of cAMP‐gated channel from bovine olfactory epithelium

Cited by 255 publications

References 23 publications

Cloning and First Functional Characterization of a Plant Cyclic Nucleotide-Gated Cation Channel

Cloning and First Functional Characterization of a Plant Cyclic Nucleotide-Gated Cation Channel

Classification and Phylogenetic Analysis of the cAMP-Dependent Protein Kinase Regulatory Subunit Family

Molecular cloning, functional expression and chromosomal localization of a human homolog of the cyclic nucleotide‐gated ion channel of retinal cone photoreceptors

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