A high affinity switch for cAMP in the HCN pacemaker channels
Abstract Binding of cAMP to Hyperpolarization activated cyclic nucleotide gated (HCN) channels facilitates pore opening. It is unclear why the isolated cyclic nucleotide binding domain (CNBD) displays in vitro lower affinity for cAMP than the full-length channel in patch experiments. Here we show th...
Main Authors: | Alessandro Porro, Andrea Saponaro, Roberta Castelli, Bianca Introini, Anahita Hafez Alkotob, Golnaz Ranjbari, Uta Enke, Jana Kusch, Klaus Benndorf, Bina Santoro, Dario DiFrancesco, Gerhard Thiel, Anna Moroni |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Portfolio
2024-01-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-024-45136-y |
Similar Items
-
cyclic AMP Regulation and Its Command in the Pacemaker Channel HCN4
by: Alessandro Porro, et al.
Published: (2020-07-01) -
A synthetic peptide that prevents cAMP regulation in mammalian hyperpolarization-activated cyclic nucleotide-gated (HCN) channels
by: Andrea Saponaro, et al.
Published: (2018-06-01) -
The HCN domain couples voltage gating and cAMP response in hyperpolarization-activated cyclic nucleotide-gated channels
by: Alessandro Porro, et al.
Published: (2019-11-01) -
Functional and structural characterization of interactions between opposite subunits in HCN pacemaker channels
by: Mahesh Kondapuram, et al.
Published: (2022-05-01) -
Uncoupling of Voltage- and Ligand-Induced Activation in HCN2 Channels by Glycine Inserts
by: Sezin Yüksel, et al.
Published: (2022-08-01)