ArticleScientific reports2016
From crystal structure of α-conotoxin GIC in complex with Ac-AChBP to molecular determinants of its high selectivity for α3β2 nAChR.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 42 citations in OpenAlex.
- In Silico Conotoxin Studies: Progress and Prospects.Molecules (Basel, Switzerland) · 2024Review
- Protein Painting Mass Spectrometry in the Discovery of Interaction Sites within the Acetylcholine Binding Protein.ACS chemical neuroscience · 2024Article
- Efficient Expression inMolecules (Basel, Switzerland) · 2024Article
- Fifty Years of Animal Toxin Research at the Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry RAS.International journal of molecular sciences · 2023Review
- Marine Origin Ligands of Nicotinic Receptors: Low Molecular Compounds, Peptides and Proteins for Fundamental Research and Practical Applications.Biomolecules · 2022Review
- High-Throughput Prediction and Design of Novel Conopeptides for Biomedical Research and Development.Biodesign research · 2022Article
- From Crystal Structures of RgIA4 in Complex withMarine drugs · 2021Article
- Rigidity of loop 1 contributes to equipotency of globular and ribbon isomers of α-conotoxin AusIA.Scientific reports · 2021Article
- Characterization of an α 4/7-Conotoxin LvIF fromMarine drugs · 2021Article
- Potency- and Selectivity-Enhancing Mutations of Conotoxins for Nicotinic Acetylcholine Receptors Can Be Predicted Using Accurate Free-Energy Calculations.Marine drugs · 2021Article
- Venom-Derived Neurotoxins Targeting Nicotinic Acetylcholine Receptors.Molecules (Basel, Switzerland) · 2021Review
- Unique Pharmacological Properties of α-Conotoxin OmIA at α7 nAChRs.Frontiers in pharmacology · 2021Article
- Interaction of α9α10 Nicotinic Receptors With Peptides and Proteins From Animal Venoms.Frontiers in cellular neuroscience · 2021Article
- Article
- An Investigation of Three-Finger Toxin-nAChR Interactions through Rosetta Protein Docking.Toxins · 2020Article
- Structure-Function of Neuronal Nicotinic Acetylcholine Receptor Inhibitors Derived From Natural Toxins.Frontiers in neuroscience · 2020Review
- ConoMode, a database for conopeptide binding modes.Database : the journal of biological databases and curation · 2020Article
- In Silico Modeling of the α7 Nicotinic Acetylcholine Receptor: New Pharmacological Challenges Associated with Multiple Modes of Signaling.Mini reviews in medicinal chemistry · 2020Review
- Structural and Functional Analyses of Cone Snail Toxins.Marine drugs · 2019Review
- Snails In Silico: A Review of Computational Studies on the Conopeptides.Marine drugs · 2019Review
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Authors and funding
12 authors at 4 institutions in 3 countries.
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Abstract
Acetylcholine binding proteins (AChBPs) are unique spatial homologs of the ligand-binding domains of nicotinic acetylcholine receptors (nAChRs), and they reproduce some pharmacological properties of nAChRs. X-ray crystal structures of AСhBP in complex with α-conotoxins provide important insights into the interactions of α-conotoxins with distinct nAChR subtypes. Although considerable efforts have been made to understand why α-conotoxin GIC is strongly selective for α3β2 nAChR, this question has not yet been solved. Here we present the structure of α-conotoxin GIC in complex with Aplysia californica AChBP (Ac-AChBP) at a resolution of 2.1 Å. Based on this co-crystal structure complemented with molecular docking data, we suggest the key residues of GIC in determining its high affinity and selectivity for human α3β2 vs α3β4 nAChRs. These suggestions were checked by radioligand and electrophysiology experiments, which confirmed the functional role of detected contacts for GIC interactions with Ac-AChBP and α3β2 nAChR subtypes. While GIC elements responsible for its high affinity binding with Ac-AChBP and α3β2 nAChR were identified, our study also showed the limitations of computer modelling in extending the data from the X-ray structures of the AChBP complexes to all nAChR subtypes.
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