Structural determinants of selective alpha-conotoxin binding to a nicotinic acetylcholine receptor homolog AChBP

C. Ulens; R.C. Hogg; P.H. Celie; D. Bertrand; V. Tsetlin; A.B. Smit; T.K. Sixma

doi:10.1073/pnas.0507889103

Structural determinants of selective alpha-conotoxin binding to a nicotinic acetylcholine receptor homolog AChBP

C. Ulens
, R.C. Hogg
, P.H. Celie
, D. Bertrand
, V. Tsetlin
, A.B. Smit
, T.K. Sixma

Molecular and Cellular Neurobiology

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

Abstract

The nicotinic acetylcholine receptor (nAChR) is the prototype member of the super-family of pentameric ligand-gated ion channels. How the extracellular ligand-binding domain coordinates selective binding of ligand molecules to different subtypes of the receptor is unknown at the structural level. Here, we present the 2.2-Å crystal structure of a homolog of the ligand-binding domain of the nAChR, Aplysia californica AChBP (Ac-AChBP), in complex with α-conotoxin ImI. This conotoxin is unique in its selectivity toward the neuronal α

Original language	English
Pages (from-to)	3615-3620
Number of pages	6
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	103
DOIs	https://doi.org/10.1073/pnas.0507889103
Publication status	Published - 2006

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10.1073/pnas.0507889103

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abstract = "The nicotinic acetylcholine receptor (nAChR) is the prototype member of the super-family of pentameric ligand-gated ion channels. How the extracellular ligand-binding domain coordinates selective binding of ligand molecules to different subtypes of the receptor is unknown at the structural level. Here, we present the 2.2-{\AA} crystal structure of a homolog of the ligand-binding domain of the nAChR, Aplysia californica AChBP (Ac-AChBP), in complex with α-conotoxin ImI. This conotoxin is unique in its selectivity toward the neuronal α",

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AU - Ulens, C.

AU - Hogg, R.C.

AU - Celie, P.H.

AU - Bertrand, D.

AU - Tsetlin, V.

AU - Smit, A.B.

AU - Sixma, T.K.

PY - 2006

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AB - The nicotinic acetylcholine receptor (nAChR) is the prototype member of the super-family of pentameric ligand-gated ion channels. How the extracellular ligand-binding domain coordinates selective binding of ligand molecules to different subtypes of the receptor is unknown at the structural level. Here, we present the 2.2-Å crystal structure of a homolog of the ligand-binding domain of the nAChR, Aplysia californica AChBP (Ac-AChBP), in complex with α-conotoxin ImI. This conotoxin is unique in its selectivity toward the neuronal α

U2 - 10.1073/pnas.0507889103

DO - 10.1073/pnas.0507889103

M3 - Article

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JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

ER -

Structural determinants of selective alpha-conotoxin binding to a nicotinic acetylcholine receptor homolog AChBP

Abstract

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