| 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 - Sixma_2003_Annu.Rev.Biophys.Biomol.Struct_32_311 |
| Author(s) : Sixma TK , Smit AB |
| Ref : Annu Rev Biophys Biomol Struct , 32 :311 , 2003 |
|
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. |
| PubMedSearch : Sixma_2003_Annu.Rev.Biophys.Biomol.Struct_32_311 |
| PubMedID: 12695308 |
Sixma TK, Smit AB (2003)
Acetylcholine binding protein (AChBP): a secreted glial protein that provides a high-resolution model for the extracellular domain of pentameric ligand-gated ion channels
Annu Rev Biophys Biomol Struct
32 :311
Sixma TK, Smit AB (2003)
Annu Rev Biophys Biomol Struct
32 :311