Crystal structure of nicotinic acetylcholine receptor homolog AChBP in complex with an alpha-conotoxin PnIA variant

P.H.N. Celie; I.E. Kasheverov; D.Y. Mordventisev; R.C. Hogg; P. van Nierop; R. van Elk; S.E. van Rossum-Fikkert; M.N. Zhmak; D. Bertrand; V. Tsetlin; T.K. Sixma; A.B. Smit

doi:10.1038/nsmb951

Crystal structure of nicotinic acetylcholine receptor homolog AChBP in complex with an alpha-conotoxin PnIA variant

P.H.N. Celie, I.E. Kasheverov, D.Y. Mordventisev, R.C. Hogg, P. van Nierop, R. van Elk, S.E. van Rossum-Fikkert, M.N. Zhmak, D. Bertrand, V. Tsetlin, T.K. Sixma, A.B. Smit

Molecular and Cellular Neurobiology

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

Abstract

Conotoxins (Ctx) form a large family of peptide toxins from cone snail venoms that act on a broad spectrum of ion channels and receptors. The subgroup α-Ctx specifically and selectively binds to subtypes of nicotinic acetylcholine receptors (nAChRs), which are targets for treatment of several neurological disorders. Here we present the structure at a resolution of 2.4 Å of α-Ctx PnIA (A10L D14K), a potent blocker of the α

Original language	English
Pages (from-to)	582-588
Number of pages	7
Journal	Nature Structural and Molecular Biology
Volume	12
Issue number	7
DOIs	https://doi.org/10.1038/nsmb951
Publication status	Published - 2005

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Celie, P. H. N., Kasheverov, I. E., Mordventisev, D. Y., Hogg, R. C., van Nierop, P., van Elk, R., van Rossum-Fikkert, S. E., Zhmak, M. N., Bertrand, D., Tsetlin, V., Sixma, T. K., & Smit, A. B. (2005). Crystal structure of nicotinic acetylcholine receptor homolog AChBP in complex with an alpha-conotoxin PnIA variant. Nature Structural and Molecular Biology, 12(7), 582-588. https://doi.org/10.1038/nsmb951

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title = "Crystal structure of nicotinic acetylcholine receptor homolog AChBP in complex with an alpha-conotoxin PnIA variant",

abstract = "Conotoxins (Ctx) form a large family of peptide toxins from cone snail venoms that act on a broad spectrum of ion channels and receptors. The subgroup α-Ctx specifically and selectively binds to subtypes of nicotinic acetylcholine receptors (nAChRs), which are targets for treatment of several neurological disorders. Here we present the structure at a resolution of 2.4 {\AA} of α-Ctx PnIA (A10L D14K), a potent blocker of the α",

author = "P.H.N. Celie and I.E. Kasheverov and D.Y. Mordventisev and R.C. Hogg and {van Nierop}, P. and {van Elk}, R. and {van Rossum-Fikkert}, S.E. and M.N. Zhmak and D. Bertrand and V. Tsetlin and T.K. Sixma and A.B. Smit",

year = "2005",

doi = "10.1038/nsmb951",

language = "English",

volume = "12",

pages = "582--588",

journal = "Nature Structural and Molecular Biology",

issn = "1545-9993",

publisher = "Nature Publishing Group",

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Celie, PHN, Kasheverov, IE, Mordventisev, DY, Hogg, RC, van Nierop, P, van Elk, R, van Rossum-Fikkert, SE, Zhmak, MN, Bertrand, D, Tsetlin, V, Sixma, TK & Smit, AB 2005, 'Crystal structure of nicotinic acetylcholine receptor homolog AChBP in complex with an alpha-conotoxin PnIA variant', Nature Structural and Molecular Biology, vol. 12, no. 7, pp. 582-588. https://doi.org/10.1038/nsmb951

TY - JOUR

T1 - Crystal structure of nicotinic acetylcholine receptor homolog AChBP in complex with an alpha-conotoxin PnIA variant

AU - Celie, P.H.N.

AU - Kasheverov, I.E.

AU - Mordventisev, D.Y.

AU - Hogg, R.C.

AU - van Nierop, P.

AU - van Elk, R.

AU - van Rossum-Fikkert, S.E.

AU - Zhmak, M.N.

AU - Bertrand, D.

AU - Tsetlin, V.

AU - Sixma, T.K.

AU - Smit, A.B.

PY - 2005

Y1 - 2005

N2 - Conotoxins (Ctx) form a large family of peptide toxins from cone snail venoms that act on a broad spectrum of ion channels and receptors. The subgroup α-Ctx specifically and selectively binds to subtypes of nicotinic acetylcholine receptors (nAChRs), which are targets for treatment of several neurological disorders. Here we present the structure at a resolution of 2.4 Å of α-Ctx PnIA (A10L D14K), a potent blocker of the α

AB - Conotoxins (Ctx) form a large family of peptide toxins from cone snail venoms that act on a broad spectrum of ion channels and receptors. The subgroup α-Ctx specifically and selectively binds to subtypes of nicotinic acetylcholine receptors (nAChRs), which are targets for treatment of several neurological disorders. Here we present the structure at a resolution of 2.4 Å of α-Ctx PnIA (A10L D14K), a potent blocker of the α

U2 - 10.1038/nsmb951

DO - 10.1038/nsmb951

M3 - Article

VL - 12

SP - 582

EP - 588

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

SN - 1545-9993

IS - 7

ER -

Crystal structure of nicotinic acetylcholine receptor homolog AChBP in complex with an alpha-conotoxin PnIA variant

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