Weißgraeber, Stephanie ; Saponaro, Andrea ; Thiel, Gerhard ; Hamacher, Kay (2017)
A reduced mechanical model for cAMP-modulated gating in HCN channels.
In: Scientific reports, 7
Artikel, Bibliographie
Kurzbeschreibung (Abstract)
We developed an in silico mechanical model to analyze the process of cAMP-induced conformational modulations in hyperpolarization-activated cyclic nucleotide-gated (HCN) channels, which conduct cations across the membrane of mammalian heart and brain cells. The structural analysis reveals a quaternary twist in the cytosolic parts of the four subunits in the channel tetramer. This motion augments the intrinsic dynamics of the very same protein structure. The pronounced differences between the cAMP bound and unbound form include a mutual interaction between the C-linker of the cyclic nucleotide binding domain (CNBD) and the linker between the S4 and S5 transmembrane domain of the channel. This allows a mechanistic annotation of the twisting motion in relation to the allosteric modulation of voltage-dependent gating of this channel by cAMP.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2017 |
| Autor(en): | Weißgraeber, Stephanie ; Saponaro, Andrea ; Thiel, Gerhard ; Hamacher, Kay |
| Art des Eintrags: | Bibliographie |
| Titel: | A reduced mechanical model for cAMP-modulated gating in HCN channels. |
| Sprache: | Englisch |
| Publikationsjahr: | 11 Januar 2017 |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Scientific reports |
| Jahrgang/Volume einer Zeitschrift: | 7 |
| Kurzbeschreibung (Abstract): | We developed an in silico mechanical model to analyze the process of cAMP-induced conformational modulations in hyperpolarization-activated cyclic nucleotide-gated (HCN) channels, which conduct cations across the membrane of mammalian heart and brain cells. The structural analysis reveals a quaternary twist in the cytosolic parts of the four subunits in the channel tetramer. This motion augments the intrinsic dynamics of the very same protein structure. The pronounced differences between the cAMP bound and unbound form include a mutual interaction between the C-linker of the cyclic nucleotide binding domain (CNBD) and the linker between the S4 and S5 transmembrane domain of the channel. This allows a mechanistic annotation of the twisting motion in relation to the allosteric modulation of voltage-dependent gating of this channel by cAMP. |
| ID-Nummer: | pmid:28074902 |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie 10 Fachbereich Biologie > Plant Membrane Biophyscis (am 20.12.23 umbenannt in Biologie der Algen und Protozoen) 10 Fachbereich Biologie > Computational Biology and Simulation |
| Hinterlegungsdatum: | 24 Jan 2017 13:33 |
| Letzte Änderung: | 24 Apr 2018 08:06 |
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