Unraveling the modular design of glutamate-gated ion channels.
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.
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Dept of Pharmacology, Cornell University, Ithaca, NY 14853, USA.
Oswald
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D000595:Amino Acid Sequence; D000818:Animals; D005075:Biological Evolution; D018698:Glutamic Acid / Q000502:physiology*; D006801:Humans; D015640:Ion Channel Gating; D007473:Ion Channels / Q000235:genetics / Q000502:physiology*; D008024:Ligands; D008969:Molecular Sequence Data
D007473:Ion Channels; D008024:Ligands; D018698:Glutamic Acid