Crystal structure of nicotinic acetylcholine receptor homolog AChBP in complex with an alpha-conotoxin PnIA variant. (Q46542399)

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12 January 2020

title

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

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12 January 2020

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author name string

Patrick H N Celie

1

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Igor E Kasheverov

2

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Dmitry Y Mordvintsev

3

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Ronald C Hogg

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Pim van Nierop

5

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René van Elk

6

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Sarah E van Rossum-Fikkert

7

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Maxim N Zhmak

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Daniel Bertrand

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Victor Tsetlin

10

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August B Smit

12

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publication date

12 June 2005

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Nature Structural & Molecular Biology

12 January 2020

published in

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volume

12

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issue

7

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page(s)

582-588

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https://scigraph.springernature.com/pub.10.1038/nsmb951

12 January 2020

exact match

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Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors

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Homology model of the GABAA receptor examined using Brownian dynamics

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Single-residue alteration in alpha-conotoxin PnIA switches its nAChR subtype selectivity.

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Single Amino Acid Substitutions in α-Conotoxin PnIA Shift Selectivity for Subtypes of the Mammalian Neuronal Nicotinic Acetylcholine Receptor

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Alpha-conotoxins PnIA and [A10L]PnIA stabilize different states of the alpha7-L247T nicotinic acetylcholine receptor.

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Unconventional pharmacology of a neuronal nicotinic receptor mutated in the channel domain

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Crystal structure of acetylcholine-binding protein from Bulinus truncatus reveals the conserved structural scaffold and sites of variation in nicotinic acetylcholine receptors.

31 March 2020

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The 1.1 A crystal structure of the neuronal acetylcholine receptor antagonist, alpha-conotoxin PnIA from Conus pennaceus

31 March 2020

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Crystal structure at 1.1 A resolution of alpha-conotoxin PnIB: comparison with alpha-conotoxins PnIA and GI

31 March 2020

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Computational approaches to understand alpha-conotoxin interactions at neuronal nicotinic receptors

31 March 2020

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Invariant aspartic Acid in muscle nicotinic receptor contributes selectively to the kinetics of agonist binding

31 March 2020

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Models of the extracellular domain of the nicotinic receptors and of agonist- and Ca2+-binding sites

31 March 2020

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Identification of tyrosine sulfation inConuspennaceus conotoxins α-PnIA and α-PnIB: further investigation of labile sulfo- and phosphopeptides by electrospray, matrix-assisted laser desorption/ionization (MALDI) and atmospheric pressure MALDI mass

31 March 2020

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Pairwise interactions between neuronal alpha(7) acetylcholine receptors and alpha-conotoxin PnIB.

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Agonist-mediated conformational changes in acetylcholine-binding protein revealed by simulation and intrinsic tryptophan fluorescence

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Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake alpha-neurotoxins and nicotinic receptors.

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Leu(10) of alpha-conotoxin PnIB confers potency for neuronal nicotinic responses in bovine chromaffin cells

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Activation of the nicotinic acetylcholine receptor involves a switch in conformation of the alpha subunits.

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Structure and gating mechanism of the acetylcholine receptor pore

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Snake venom toxins, unlike smaller antagonists, appear to stabilize a resting state conformation of the nicotinic acetylcholine receptor

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Photoactivatable alpha-conotoxins reveal contacts with all subunits as well as antagonist-induced rearrangements in the Torpedo californica acetylcholine receptor

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Refined structure of the nicotinic acetylcholine receptor at 4A resolution

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SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling

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31 March 2020

Identifiers

DOI

10.1038/NSMB951

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12 January 2020

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