Structure and function of AChBP, homologue of the ligand-binding domain of the nicotinic acetylcholine receptor

A.B. Smit; K. Brejc; N.I. Syed; T.K. Sixma

doi:10.1196/annals.1254.010

Structure and function of AChBP, homologue of the ligand-binding domain of the nicotinic acetylcholine receptor

A.B. Smit, K. Brejc, N.I. Syed, T.K. Sixma

Molecular and Cellular Neurobiology

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

Acetylcholine-binding protein (AChBP) is a novel protein with high similarity to the extracellular domain of the nicotinic acetylcholine receptor. AChBP lacks the transmembrane domains and intracellular loops typical for the nAChRs. AChBP is secreted from glia cells in the central nervous system of the freshwater snail, Lymnaea stagnalis, where it modulates synaptic transmission. AChBP forms homopentamers with pharmacology that resembles the α

Original language	English
Pages (from-to)	81-92
Number of pages	12
Journal	Annals of the New York Academy of Sciences
Volume	998
DOIs	https://doi.org/10.1196/annals.1254.010
Publication status	Published - 2003

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title = "Structure and function of AChBP, homologue of the ligand-binding domain of the nicotinic acetylcholine receptor",

abstract = "Acetylcholine-binding protein (AChBP) is a novel protein with high similarity to the extracellular domain of the nicotinic acetylcholine receptor. AChBP lacks the transmembrane domains and intracellular loops typical for the nAChRs. AChBP is secreted from glia cells in the central nervous system of the freshwater snail, Lymnaea stagnalis, where it modulates synaptic transmission. AChBP forms homopentamers with pharmacology that resembles the α",

author = "A.B. Smit and K. Brejc and N.I. Syed and T.K. Sixma",

year = "2003",

doi = "10.1196/annals.1254.010",

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AU - Smit, A.B.

AU - Brejc, K.

AU - Syed, N.I.

AU - Sixma, T.K.

PY - 2003

Y1 - 2003

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AB - Acetylcholine-binding protein (AChBP) is a novel protein with high similarity to the extracellular domain of the nicotinic acetylcholine receptor. AChBP lacks the transmembrane domains and intracellular loops typical for the nAChRs. AChBP is secreted from glia cells in the central nervous system of the freshwater snail, Lymnaea stagnalis, where it modulates synaptic transmission. AChBP forms homopentamers with pharmacology that resembles the α

U2 - 10.1196/annals.1254.010

DO - 10.1196/annals.1254.010

M3 - Article

SN - 0077-8923

VL - 998

SP - 81

EP - 92

JO - Annals of the New York Academy of Sciences

JF - Annals of the New York Academy of Sciences

ER -

Structure and function of AChBP, homologue of the ligand-binding domain of the nicotinic acetylcholine receptor

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