Journal article
The structure of the apo cAMP‐binding domain of HCN4 – a stepping stone toward understanding the cAMP‐dependent modulation of the hyperpolarization‐activated cyclic‐nucleotide‐gated ion channels
Abstract
The hyperpolarization-activated cyclic-nucleotide-gated (HCN) ion channels control nerve impulse transmission and cardiac pacemaker activity. The modulation by cAMP is critical for the regulatory function of HCN in both neurons and cardiomyocytes, but the underlying mechanism is not fully understood. Here, we show how the structure of the apo cAMP-binding domain of the HCN4 isoform has contributed to a model for the cAMP-dependent modulation of …
Authors
Akimoto M; VanSchouwen B; Melacini G
Journal
The FEBS Journal, Vol. 285, No. 12, pp. 2182–2192
Publisher
Wiley
Publication Date
6 2018
DOI
10.1111/febs.14408
ISSN
1742-464X
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
Allosteric RegulationAmino Acid MotifsBinding SitesCrystallography, X-RayCyclic AMPCyclic GMPGene ExpressionHumansHyperpolarization-Activated Cyclic Nucleotide-Gated ChannelsIon Channel GatingModels, MolecularMuscle ProteinsPotassiumPotassium ChannelsProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsProtein MultimerizationProtein Structure, TertiaryRecombinant ProteinsThermodynamics