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- W1967368966 endingPage "334" @default.
- W1967368966 startingPage "311" @default.
- W1967368966 abstract "Acetylcholine binding protein (AChBP) has recently been identified from molluskan glial cells. Glial cells secrete it into cholinergic synapses, where it plays a role in modulating synaptic transmission. This novel mechanism resembles glia-dependent modulation of glutamate synapses, with several key differences. AChBP is a homolog of the ligand binding domain of the pentameric ligand-gated ion-channels. The crystal structure of AChBP provides the first high-resolution structure for this family of Cys-loop receptors. Nicotinic acetylcholine receptors and related ion-channels such as GABAA, serotonin 5HT3, and glycine can be interpreted in the light of the 2.7 A AChBP structure. The structural template provides critical details of the binding site and helps create models for toxin binding, mutational effects, and molecular gating." @default.
- W1967368966 created "2016-06-24" @default.
- W1967368966 creator A5003301414 @default.
- W1967368966 creator A5046661343 @default.
- W1967368966 date "2003-06-01" @default.
- W1967368966 modified "2023-10-16" @default.
- W1967368966 title "Acetylcholine Binding Protein (AChBP): A Secreted Glial Protein That Provides a High-Resolution Model for the Extracellular Domain of Pentameric Ligand-Gated Ion Channels" @default.
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