title: Structural snapshot of cyclic nucleotide binding domains from cyclic nucleotide-sensitive ion channels.
abstract: Cyclic nucleotide-binding domains (CNBDs) that are present in various channel proteins play crucial roles in signal amplification cascades. Although atomic resolution structures of some of those CNBDs are available, the detailed mechanism by which they confer cyclic nucleotide-binding to the ion channel pore remains poorly understood. In this review, we describe structural insights about cyclic nucleotide-binding-induced conformational changes in CNBDs and their potential coupling with channel gating.
authors.forename: Sven
authors.initials: S
authors.lastname: Schünke
authors.forename: Matthias
authors.initials: M
authors.lastname: Stoldt
mesh_terms: D000818:Animals; D015220:Calcium Channels / Q000737:chemistry / Q000378:metabolism; D000242:Cyclic AMP / Q000737:chemistry / Q000378:metabolism; D054815:Cyclic Nucleotide-Gated Cation Channels / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008024:Ligands; D059128:Mesorhizobium / Q000737:chemistry / Q000378:metabolism; D024642:Potassium Channels, Voltage-Gated / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary; D015222:Sodium Channels / Q000737:chemistry / Q000378:metabolism; D013329:Structure-Activity Relationship
chemical_list: D015220:Calcium Channels; D054815:Cyclic Nucleotide-Gated Cation Channels; D008024:Ligands; D024642:Potassium Channels, Voltage-Gated; D015222:Sodium Channels; D000242:Cyclic AMP