Functional and structural characterization of interactions between opposite subunits in HCN pacemaker channels
Hyperpolarization-activated and cyclic nucleotide (HCN) modulated channels are tetrameric cation channels. In each of the four subunits, the intracellular cyclic nucleotide-binding domain (CNBD) is coupled to the transmembrane domain via a helical structure, the C-linker. High-resolution channel str...
Main Authors: | Benndorf, K. (Author), Frieg, B. (Author), Gohlke, H. (Author), Kondapuram, M. (Author), Kusch, J. (Author), Lelle, M. (Author), Sattler, C. (Author), Schmauder, R. (Author), Schwabe, T. (Author), Schweinitz, A. (Author), Yüksel, S. (Author) |
---|---|
Format: | Article |
Language: | English |
Published: |
NLM (Medline)
2022
|
Online Access: | View Fulltext in Publisher |
Similar Items
-
Probability fluxes and transition paths in a Markovian model describing complex subunit cooperativity in HCN2 channels.
by: Klaus Benndorf, et al.
Published: (2012-01-01) -
Activation gating in HCN2 channels.
by: Sabine Hummert, et al.
Published: (2018-03-01) -
Gating mechanism of hyperpolarization-activated HCN pacemaker channels
by: Rosamary Ramentol, et al.
Published: (2020-03-01) -
Molecular mechanism of cyclic nucleotide action on HCN pacemaker channels
by: Ng, Leo Chun Ting
Published: (2016) -
Unravelling the intricate cooperativity of subunit gating in P2X2 ion channels
by: Christian Sattler, et al.
Published: (2020-12-01)