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| Hauptseite > Publikationsdatenbank > Functional and structural characterization of interactions between opposite subunits in HCN pacemaker channels > print |
| Hauptseite > Publikationsdatenbank > Functional and structural characterization of interactions between opposite subunits in HCN pacemaker channels > print |
| 001 | 907779 | ||
| 005 | 20230128125811.0 | ||
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| 100 | 1 | _ | |a Kondapuram, Mahesh |0 0000-0002-9287-7189 |b 0 |
| 245 | _ | _ | |a Functional and structural characterization of interactions between opposite subunits in HCN pacemaker channels |
| 260 | _ | _ | |a London |c 2022 |b Springer Nature |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 520 | _ | _ | |a 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 structures suggest that the C-linker enables functionally relevant interactions with the opposite subunit, which might be critical for coupling the conformational changes in the CNBD to the channel pore. We combined mutagenesis, patch-clamp technique, confocal patch-clamp fluorometry, and molecular dynamics (MD) simulations to show that residue K464 of the C-linker is relevant for stabilizing the closed state of the mHCN2 channel by forming interactions with the opposite subunit. MD simulations revealed that in the K464E channel, a rotation of the intracellular domain relative to the channel pore is induced, which is similar to the cAMP-induced rotation, weakening the autoinhibitory effect of the unoccupied CL-CNBD region. We suggest that this CL-CNBD rotation is considerably involved in activation-induced affinity increase but only indirectly involved in gate modulation. The adopted poses shown herein are in excellent agreement with previous structural results. |
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| 700 | 1 | _ | |a Gohlke, Holger |0 P:(DE-Juel1)172663 |b 9 |e Corresponding author |
| 700 | 1 | _ | |a Kusch, Jana |0 0000-0001-7206-8133 |b 10 |e Corresponding author |
| 773 | _ | _ | |a 10.1038/s42003-022-03360-6 |g Vol. 5, no. 1, p. 430 |0 PERI:(DE-600)2919698-X |n 1 |p 430 |t Communications biology |v 5 |y 2022 |x 2399-3642 |
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