AChBP-targeted alpha-conotoxin correlates distinct binding orientations with nAChR subtype selectivity

S. Dutertre; C. Ulens; R. Buttner; A. Fish; R. van Elk; Y. Kendel; G. Hopping; P.F. Alewood; C. Schroeder; A. Nicke; A.B. Smit; T.K. Sixma; R.J. Lewis

doi:10.1038/sj.emboj.7601785

AChBP-targeted alpha-conotoxin correlates distinct binding orientations with nAChR subtype selectivity

S. Dutertre, C. Ulens, R. Buttner, A. Fish, R. van Elk, Y. Kendel, G. Hopping, P.F. Alewood, C. Schroeder, A. Nicke, A.B. Smit, T.K. Sixma, R.J. Lewis

Molecular and Cellular Neurobiology

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

Abstract

Neuronal nAChRs are a diverse family of pentameric ion channels with wide distribution throughout cells of the nervous and immune systems. However, the role of specific subtypes in normal and pathological states remains poorly understood due to the lack of selective probes. Here, we used a binding assay based on acetylcholine-binding protein (AChBP), a homolog of the nicotinic acetylcholine ligand-binding domain, to discover a novel α-conotoxin (α-TxIA) in the venom of Conus textile. α-TxIA bound with high affinity to AChBPs from different species and selectively targeted the α

Original language	English
Pages (from-to)	3858-3867
Journal	EMBO Journal
Volume	26
Issue number	16
DOIs	https://doi.org/10.1038/sj.emboj.7601785
Publication status	Published - 2007

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10.1038/sj.emboj.7601785

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@article{d73b42b068684776a4475f5055e30043,

title = "AChBP-targeted alpha-conotoxin correlates distinct binding orientations with nAChR subtype selectivity",

abstract = "Neuronal nAChRs are a diverse family of pentameric ion channels with wide distribution throughout cells of the nervous and immune systems. However, the role of specific subtypes in normal and pathological states remains poorly understood due to the lack of selective probes. Here, we used a binding assay based on acetylcholine-binding protein (AChBP), a homolog of the nicotinic acetylcholine ligand-binding domain, to discover a novel α-conotoxin (α-TxIA) in the venom of Conus textile. α-TxIA bound with high affinity to AChBPs from different species and selectively targeted the α",

author = "S. Dutertre and C. Ulens and R. Buttner and A. Fish and {van Elk}, R. and Y. Kendel and G. Hopping and P.F. Alewood and C. Schroeder and A. Nicke and A.B. Smit and T.K. Sixma and R.J. Lewis",

year = "2007",

doi = "10.1038/sj.emboj.7601785",

language = "English",

volume = "26",

pages = "3858--3867",

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issn = "0261-4189",

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T1 - AChBP-targeted alpha-conotoxin correlates distinct binding orientations with nAChR subtype selectivity

AU - Dutertre, S.

AU - Ulens, C.

AU - Buttner, R.

AU - Fish, A.

AU - van Elk, R.

AU - Kendel, Y.

AU - Hopping, G.

AU - Alewood, P.F.

AU - Schroeder, C.

AU - Nicke, A.

AU - Smit, A.B.

AU - Sixma, T.K.

AU - Lewis, R.J.

PY - 2007

Y1 - 2007

N2 - Neuronal nAChRs are a diverse family of pentameric ion channels with wide distribution throughout cells of the nervous and immune systems. However, the role of specific subtypes in normal and pathological states remains poorly understood due to the lack of selective probes. Here, we used a binding assay based on acetylcholine-binding protein (AChBP), a homolog of the nicotinic acetylcholine ligand-binding domain, to discover a novel α-conotoxin (α-TxIA) in the venom of Conus textile. α-TxIA bound with high affinity to AChBPs from different species and selectively targeted the α

AB - Neuronal nAChRs are a diverse family of pentameric ion channels with wide distribution throughout cells of the nervous and immune systems. However, the role of specific subtypes in normal and pathological states remains poorly understood due to the lack of selective probes. Here, we used a binding assay based on acetylcholine-binding protein (AChBP), a homolog of the nicotinic acetylcholine ligand-binding domain, to discover a novel α-conotoxin (α-TxIA) in the venom of Conus textile. α-TxIA bound with high affinity to AChBPs from different species and selectively targeted the α

U2 - 10.1038/sj.emboj.7601785

DO - 10.1038/sj.emboj.7601785

M3 - Article

SN - 0261-4189

VL - 26

SP - 3858

EP - 3867

JO - EMBO Journal

JF - EMBO Journal

IS - 16

ER -

AChBP-targeted alpha-conotoxin correlates distinct binding orientations with nAChR subtype selectivity

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