TY - JOUR
T1 - Acetylcholine binding protein (AChBP): A secreted glial protein that provides a high-resolution model for the extracellular domain of pentameric ligand-gated ion channels
AU - Sixma, T.K.
AU - Smit, A.B.
PY - 2003
Y1 - 2003
N2 - 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 GABA
AB - 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 GABA
UR - https://www.scopus.com/pages/publications/0041352143
UR - https://www.scopus.com/inward/citedby.url?scp=0041352143&partnerID=8YFLogxK
U2 - 10.1146/annurev.biophys.32.110601.142536
DO - 10.1146/annurev.biophys.32.110601.142536
M3 - Article
SN - 1056-8700
VL - 32
SP - 311
EP - 334
JO - Annual Review of Biophysics and Biomolecular Structure
JF - Annual Review of Biophysics and Biomolecular Structure
ER -
