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- W2255030827 abstract "The role of the outermost transmembrane α-helix in both the maturation and function of the prokaryotic pentameric ligand-gated ion channels, GLIC and ELIC, was examined by Ala scanning mutagenesis, deletion mutations, and mutant cycle analyses. Ala mutations at the M4-M1/M3 interface lead to loss-of-function phenotypes in GLIC, with the largest negative effects occurring near the M4 C terminus. In particular, two aromatic residues at the M4 C terminus form a network of π-π and/or cation-π interactions with residues on M3 and the β6-β7 loop that is essential for both maturation and function. M4-M1/M3 interactions appear to be optimized in GLIC with even subtle structural changes at this interface leading to detrimental effects. In contrast, mutations along the M4-M1/M3 interface of ELIC typically lead to gain-of-function phenotypes, suggesting that these interactions in ELIC are not optimized for channel function. In addition, no cluster of interacting residues involving the M4 C terminus, M3, and the β6-β7 loop was found, suggesting that the M4 C terminus plays little role in ELIC maturation or function. This study shows that M4 makes distinct contributions to the maturation and gating of these two closely related homologs, suggesting that GLIC and ELIC exhibit divergent features of channel function." @default.
- W2255030827 created "2016-06-24" @default.
- W2255030827 creator A5005757714 @default.
- W2255030827 creator A5029690483 @default.
- W2255030827 creator A5063092943 @default.
- W2255030827 date "2015-10-01" @default.
- W2255030827 modified "2023-09-26" @default.
- W2255030827 title "The M4 Transmembrane α-Helix Contributes Differently to Both the Maturation and Function of Two Prokaryotic Pentameric Ligand-gated Ion Channels" @default.
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- W2255030827 doi "https://doi.org/10.1074/jbc.m115.676833" @default.
- W2255030827 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4599015" @default.
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- W2255030827 hasPublicationYear "2015" @default.
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