Coupling of a viral K+-channel with a glutamate-binding-domain highlights the modular design of ionotropic glutamate-receptors View Full Text


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Article Info

DATE

2019-12

AUTHORS

Michael Schönrock, Gerhard Thiel, Bodo Laube

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 KcvATCV-1 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 KcvATCV-1. 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. More... »

PAGES

75

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s42003-019-0320-y

DOI

http://dx.doi.org/10.1038/s42003-019-0320-y

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1112308410

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30820470


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