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| Hauptseite > Externe Publikationen > Vita Publikationen > Functional and structural characterization of interactions between opposite subunits in HCN pacemaker channels > print |
| Hauptseite > Externe Publikationen > Vita Publikationen > Functional and structural characterization of interactions between opposite subunits in HCN pacemaker channels > print |
| 001 | 890666 | ||
| 005 | 20210222133906.0 | ||
| 024 | 7 | _ | |a 10.1101/2020.09.21.305797 |2 doi |
| 024 | 7 | _ | |a 0022-7722 |2 ISSN |
| 024 | 7 | _ | |a 1447-073X |2 ISSN |
| 024 | 7 | _ | |a 1447-6959 |2 ISSN |
| 037 | _ | _ | |a FZJ-2021-01114 |
| 082 | _ | _ | |a 570 |
| 100 | 1 | _ | |a Kondapuram, Mahesh |b 0 |
| 245 | _ | _ | |a Functional and structural characterization of interactions between opposite subunits in HCN pacemaker channels |
| 260 | _ | _ | |a Cold Spring Harbor |c 2020 |b Cold Spring Harbor Laboratory, NY |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1613994807_16294 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 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 simulations to show that residue K464 of the C-linker is essential for stabilizing the closed state of the mHCN2 channel by forming interactions with the opposite subunit. MD simulations revealed that both cAMP and K464E induce a rotation of the intracellular domain relative to the channel pore, weakening the autoinhibitory effect of the unoccupied CL-CNBD region. The adopted poses are in excellent agreement with structural results. |
| 588 | _ | _ | |a Dataset connected to CrossRef |
| 700 | 1 | _ | |a Frieg, Benedikt |0 P:(DE-Juel1)172887 |b 1 |
| 700 | 1 | _ | |a Yüksel, Sezin |b 2 |
| 700 | 1 | _ | |a Schwabe, Tina |b 3 |
| 700 | 1 | _ | |a Sattler, Christian |b 4 |
| 700 | 1 | _ | |a Lelle, Marco |b 5 |
| 700 | 1 | _ | |a Schweinitz, Andrea |b 6 |
| 700 | 1 | _ | |a Schmauder, Ralf |b 7 |
| 700 | 1 | _ | |a Benndorf, Klaus |0 0000-0002-0707-4083 |b 8 |
| 700 | 1 | _ | |a Gohlke, Holger |0 P:(DE-Juel1)172663 |b 9 |
| 700 | 1 | _ | |a Kusch, Jana |0 0000-0001-7206-8133 |b 10 |
| 773 | _ | _ | |a 10.1101/2020.09.21.305797 |0 PERI:(DE-600)2766415-6 |t bioRxiv beta |y 2020 |
| 909 | C | O | |o oai:juser.fz-juelich.de:890666 |p extern4vita |
| 910 | 1 | _ | |a Forschungszentrum Jülich |0 I:(DE-588b)5008462-8 |k FZJ |b 1 |6 P:(DE-Juel1)172887 |
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| 913 | 2 | _ | |a DE-HGF |b Programmungebundene Forschung |l ohne Programm |1 G:(DE-HGF)POF4-890 |0 G:(DE-HGF)POF4-899 |3 G:(DE-HGF)POF4 |2 G:(DE-HGF)POF4-800 |4 G:(DE-HGF)POF |v ohne Topic |x 0 |
| 920 | _ | _ | |l no |
| 980 | 1 | _ | |a EXTERN4VITA |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a USER |
| 980 | _ | _ | |a I:(DE-Juel1)NIC-20090406 |
| 980 | _ | _ | |a I:(DE-Juel1)JSC-20090406 |
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