Structural snapshot of cyclic nucleotide binding domains from cyclic nucleotide-sensitive ion channels

Schünke, Sven; Stoldt, Matthias

doi:10.1515/hsz-2013-0228

Cited by 5 publications

(3 citation statements)

References 51 publications

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“…Our study reveals for the first time the structure of this region in a full-length channel context. The overall structure of the cGMP-bound CNBD of TAX-4 is similar to the ligand-bound structures of the CNBD of other cyclic-nucleotide binding proteins, including HCN channels 38 . A conserved fold consisting of four α helices (designated A, P, B and C) and eight β sheets that form a β-roll is preserved in the TAX-4 CNBD (Fig.…”

Section: The Cyclic Nucleotide-binding Domain and C-linkermentioning

confidence: 67%

Structure of a eukaryotic cyclic-nucleotide-gated channel

Zhou

Wang

et al. 2017

Nature

130

166

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Summary Cyclic nucleotide-gated (CNG) channels are essential for vision and olfaction. They belong to the voltage-gated ion channel superfamily but their activities are controlled by intracellular cyclic nucleotides instead of transmembrane voltage. Here we report a 3.5 Å-resolution single-particle electron cryomicroscopy structure of a CNG channel from C. elegans in the cGMP-bound open state. The channel has an unusual voltage-sensor-like domain (VSLD), accounting for its deficient voltage dependence. A C-terminal linker connecting S6 and the cyclic nucleotide-binding domain interacts directly with both the VSLD and pore domain, forming a gating ring that couples conformational changes triggered by cyclic nucleotide binding to the gate. The selectivity filter is lined by the carboxylate side chains of a functionally important glutamate and three rings of backbone carbonyls. This structure provides a new framework for understanding mechanisms of ion permeation, gating and channelopathy of CNG channels and cyclic nucleotide modulation of related channels.

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Section: The Cyclic Nucleotide-binding Domain and C-linkermentioning

confidence: 67%

Structure of a eukaryotic cyclic-nucleotide-gated channel

Zhou

Wang

et al. 2017

Nature

130

166

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“…Some sequences lack internal parts of C-region. Single-repeat CNBD-channel of the oomycete Aphanomyces invadans Aph2584 has a substantial deletion in C-linker and most parts of CNBD, including those participating in the formation of a cyclic nucleotide-binding site (β-strands 5–8, a phosphate-binding cassette (PBC), and α-helix C 30 ), i.e. the helixes C’–F’, β-strands 5–8, PBC, and a helix B. Tandem channels of the dinoflagellate Prorocentrum minimum also have CNBD with deletions of some structures which take part in the cyclic nucleotide binding.…”

Section: Resultsmentioning

confidence: 99%

Diversity of voltage-gated potassium channels and cyclic nucleotide-binding domain-containing channels in eukaryotes

Pozdnyakov

Safonov

Skarlato

2020

Sci Rep

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Voltage-gated potassium channels (Kv) and cyclic nucleotide-binding domain-containing cation channels HCN, CNG, and KCNH are the evolutionarily related families of ion channels in animals. Their homologues were found in several lineages of eukaryotes and prokaryotes; however, the actual phylogenetic and structural diversity of these ion channels remains unclear. In this work, we present a taxonomically broad investigation of evolutionary relationships and structural diversity of Kv, HCN, CNG, and KCNH and their homologues in eukaryotes focusing on channels from different protistan groups. We demonstrate that both groups of channels consist of a more significant number of lineages than it was shown before, and these lineages can be grouped in two clusters termed Kv-like channels and CNBD-channels. Moreover, we, for the first time, report the unusual two-repeat tandem Kv-like channels and CNBD-channels in several eukaryotic groups, i.e. dinoflagellates, oomycetes, and chlorarachniophytes. Our findings reveal still underappreciated phylogenetic and structural diversity of eukaryotic ion channel lineages.

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“…The CNBD has the same fold as that of other cyclic nucleotide-binding proteins [ 48 ]. It consists of four α helices (designated as A, P, B, and C) and eight β sheets that form a β-roll.…”

Section: Structural Features and Elementsmentioning

confidence: 99%

Structural basis of properties, mechanisms, and channelopathy of cyclic nucleotide-gated channels

Hu,

Yang

2023

Channels

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Recent years have seen an outpouring of atomic or near atomic resolution structures of cyclic nucleotide-gated (CNG) channels, captured in closed, transition, pre-open, partially open, and fully open states. These structures provide unprecedented molecular insights into the activation, assembly, architecture, regulation, and channelopathy of CNG channels, as well as mechanistic explanations for CNG channel biophysical and pharmacological properties. This article summarizes recent advances in CNG channel structural biology, describes key structural features and elements, and illuminates a detailed conformational landscape of activation by cyclic nucleotides. The review also correlates structures with findings and properties delineated in functional studies, including nonselective monovalent cation selectivity, Ca 2+ permeation and block, block by L- cis -diltiazem, location of the activation gate, lack of voltage-dependent gating, and modulation by lipids and calmodulin. A perspective on future research is also offered.

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Structural snapshot of cyclic nucleotide binding domains from cyclic nucleotide-sensitive ion channels

Cited by 5 publications

References 51 publications

Structure of a eukaryotic cyclic-nucleotide-gated channel

Structure of a eukaryotic cyclic-nucleotide-gated channel

Diversity of voltage-gated potassium channels and cyclic nucleotide-binding domain-containing channels in eukaryotes

Structural basis of properties, mechanisms, and channelopathy of cyclic nucleotide-gated channels

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