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- W2040720735 endingPage "168" @default.
- W2040720735 startingPage "161" @default.
- W2040720735 abstract "Glutamate receptors that function as ligand-gated ion channels are essential components of cell-cell communication in the nervous system. Despite a wealth of information concerning these receptors, details of their structure are just beginning to emerge. We propose that glutamate receptors comprise four modules: two modules that are related to bacterial periplasmic-binding proteins, one module that is related to the pore-forming region of K + channels, and one regulatory module of unknown origin. A K + -channel-like domain inserted into a crucial region of a periplasmic-binding protein-like domain suggests a mechanism for transduction of binding energy to channel opening. This modular design also suggests an evolutionary link between a ligand-gated ion-channel family and voltage-gated ion channels." @default.
- W2040720735 created "2016-06-24" @default.
- W2040720735 creator A5057714108 @default.
- W2040720735 creator A5081269981 @default.
- W2040720735 date "1995-04-01" @default.
- W2040720735 modified "2023-10-02" @default.
- W2040720735 title "Unraveling the modular design of glutamate-gated ion channels" @default.
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- W2040720735 doi "https://doi.org/10.1016/0166-2236(95)93895-5" @default.
- W2040720735 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7539962" @default.
- W2040720735 hasPublicationYear "1995" @default.