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  Ion channel formation by synthetic transmembrane segments of the inhibitory glycine receptor - a model study

Langosch, D., Hartung, K., Grell, E., Bamberg, E., & Betz, H. (1991). Ion channel formation by synthetic transmembrane segments of the inhibitory glycine receptor - a model study. Biochimica et Biophysica Acta-Biomembranes, 1063(1), 36-44. doi:10.1016/0005-2736(91)90350-h.

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 Creators:
Langosch, Dieter1, Author
Hartung, Klaus2, Author           
Grell, Ernst3, Author           
Bamberg, Ernst2, Author           
Betz, Heinrich1, Author
Affiliations:
1ZMBH, Universität Heidelberg, Germany, ou_persistent22              
2Transport Proteins Group, Max Planck Institute of Biophysics, Max Planck Society, ou_3273415              
3Molecular Biophysics Group, Max Planck Institute of Biophysics, Max Planck Society, ou_3264820              

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Free keywords: Channel protein; Ion channel; Glycine receptor; (Rat)
 Abstract: The inhibitory glycine receptor (GlyR) of rat spinal cord contains an intrinsic transmembrane channel mediating agonist-gated anion flux. Here, synthetic peptides modelled after the predicted transmembrane domains M2 and M4 of its ligand-binding subunit were incorporated into lipid vesicle membranes and black lipid bilayers to analyze their channel forming capabilities. Both types of peptides prohibited the establishment of, or dissipated, preexisting transmembrane potentials in the vesicle system. Incorporation of peptide M2 into the black lipid bilayer elicited randomly gated single channel events with various conductance states and life-times. Peptide M4 increased the conductance of the bilayer without producing single channels. Exchange of the terminal arginine residues of peptide M2 by glutamate resulted in a significant shift towards cation selectivity of the respective channels as compared to peptide M2. In conclusion, the peptide channels observed differed significantly from native GlyR in both conductivity and ion-selectivity indicating that individual synthetic transmembrane segments are not sufficient to mimic a channel protein composed of subunits with multiple transmembrane segments.

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Language(s): eng - English
 Dates: 1990-11-141990-08-172003-04-041991-03-18
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/0005-2736(91)90350-h
PMID: 1707671
 Degree: -

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Title: Biochimica et Biophysica Acta-Biomembranes
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 1063 (1) Sequence Number: - Start / End Page: 36 - 44 Identifier: ISSN: 0005-2736
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702