Acetylcholine binding protein (AChBP): A secreted glial protein that provides a high-resolution model for the extracellular domain of pentameric ligand-gated ion channels

被引:118
作者
Sixma, TK
Smit, AB
机构
[1] Netherlands Canc Inst, Div Mol Carcinogenesis, NL-1066 CX Amsterdam, Netherlands
[2] Vrije Univ Amsterdam, Fac Biol, Neurosci Res Inst, Dept Mol & Cellular Neurobiol, NL-1081 HV Amsterdam, Netherlands
来源
ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE | 2003年 / 32卷
关键词
nicotinic acetylcholine receptor; GABA(A); 5HT(3); glycine receptor; Cys-loop;
D O I
10.1146/annurev.biophys.32.110601.142536
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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(A), serotonin 5HT(3), and glycine can be interpreted in the light of the 2.7 Angstrom AChBP structure. The structural template provides critical details of the binding site and helps create models for toxin binding, mutational effects, and molecular gating.
引用
收藏
页码:311 / 334
页数:28
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