Schönrock, Michael ; Thiel, Gerhard ; Laube, Bodo (2019)
Coupling of a viral K+-channel with a glutamate-binding-domain highlights the modular design of ionotropic glutamate-receptors.
In: Communications biology, 2
doi: 10.1038/s42003-019-0320-y
Artikel, Bibliographie
Dies ist die neueste Version dieses Eintrags.
Kurzbeschreibung (Abstract)
Ionotropic glutamate receptors (iGluRs) mediate excitatory neuronal signaling in the mammalian CNS. These receptors are critically involved in diverse physiological processes; including learning and memory formation, as well as neuronal damage associated with neurological diseases. Based on partial sequence and structural similarities, these complex cation-permeable iGluRs are thought to descend from simple bacterial proteins emerging from a fusion of a substrate binding protein (SBP) and an inverted potassium (K)-channel. Here, we fuse the pore module of the viral K-channel Kcv to the isolated glutamate-binding domain of the mammalian iGluR subunit GluA1 which is structural homolog to SBPs. The resulting chimera (GluATCV*) is functional and displays the ligand recognition characteristics of GluA1 and the K-selectivity of Kcv. These results are consistent with a conserved activation mechanism between a glutamate-binding domain and the pore-module of a K-channel and support the expected phylogenetic link between the two protein families.
Typ des Eintrags: | Artikel |
---|---|
Erschienen: | 2019 |
Autor(en): | Schönrock, Michael ; Thiel, Gerhard ; Laube, Bodo |
Art des Eintrags: | Bibliographie |
Titel: | Coupling of a viral K+-channel with a glutamate-binding-domain highlights the modular design of ionotropic glutamate-receptors. |
Sprache: | Englisch |
Publikationsjahr: | 22 Februar 2019 |
Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Communications biology |
Jahrgang/Volume einer Zeitschrift: | 2 |
DOI: | 10.1038/s42003-019-0320-y |
Zugehörige Links: | |
Kurzbeschreibung (Abstract): | Ionotropic glutamate receptors (iGluRs) mediate excitatory neuronal signaling in the mammalian CNS. These receptors are critically involved in diverse physiological processes; including learning and memory formation, as well as neuronal damage associated with neurological diseases. Based on partial sequence and structural similarities, these complex cation-permeable iGluRs are thought to descend from simple bacterial proteins emerging from a fusion of a substrate binding protein (SBP) and an inverted potassium (K)-channel. Here, we fuse the pore module of the viral K-channel Kcv to the isolated glutamate-binding domain of the mammalian iGluR subunit GluA1 which is structural homolog to SBPs. The resulting chimera (GluATCV*) is functional and displays the ligand recognition characteristics of GluA1 and the K-selectivity of Kcv. These results are consistent with a conserved activation mechanism between a glutamate-binding domain and the pore-module of a K-channel and support the expected phylogenetic link between the two protein families. |
ID-Nummer: | pmid:30820470 |
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 > Neurophysiologie und neurosensorische Systeme |
Hinterlegungsdatum: | 05 Mär 2019 06:33 |
Letzte Änderung: | 03 Jul 2024 02:38 |
PPN: | |
Export: | |
Suche nach Titel in: | TUfind oder in Google |
Verfügbare Versionen dieses Eintrags
-
Coupling of a viral K+-channel with a glutamate-binding-domain highlights the modular design of ionotropic glutamate-receptors. (deposited 07 Apr 2019 19:55)
- Coupling of a viral K+-channel with a glutamate-binding-domain highlights the modular design of ionotropic glutamate-receptors. (deposited 05 Mär 2019 06:33) [Gegenwärtig angezeigt]
Frage zum Eintrag |
Optionen (nur für Redakteure)
Redaktionelle Details anzeigen |