ArticleJournal of molecular biology2008
The role of multiple hydrogen-bonding groups in specific alcohol binding sites in proteins: insights from structural studies of LUSH.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 77 citations in OpenAlex.
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- Revealing the pH-dependent conformational changes in sol g 2.1 protein and potential ligands binding.Scientific reports · 2024Article
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- Molecular Characterization and Expression Patterns of Two Pheromone-Binding Proteins from the Diurnal MothInternational journal of molecular sciences · 2022Article
- Mutually Exclusive Expression of Closely Related Odorant-Binding Proteins 9A and 9B in the Antenna of the Red Flour BeetleBiomolecules · 2021Article
- Identification and Functional Analysis of SlitOBP11 FromFrontiers in physiology · 2021Article
- SNARE Complex-Associated Proteins and Alcohol.Alcoholism, clinical and experimental research · 2020Review
- Coordination of the Cell Wall Integrity and High-Osmolarity Glycerol Pathways in Response to Ethanol Stress in Saccharomyces cerevisiae.Applied and environmental microbiology · 2019Article
- Bioinformatic and biochemical analysis of the key binding sites of the pheromone binding protein ofPeerJ · 2019Article
- Molecular characterization and functional differentiation of three pheromone-binding proteins from Tryporyza intacta.Scientific reports · 2018Article
- Molecular and Functional Characterization of pheromone binding protein 1 from the Oriental Fruit Moth, Grapholita molesta (Busck).Scientific reports · 2018Article
- Identification, expression and characterization of the recombinant Sol g 4.1 protein from the venom of the tropical fire antThe journal of venomous animals and toxins including tropical diseases · 2018Article
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- Binding Specificity of Two PBPs in the Yellow Peach MothFrontiers in physiology · 2018Article
- Key site residues of pheromone-binding protein 1 involved in interacting with sex pheromone components of Helicoverpa armigera.Scientific reports · 2017Article
- Structural Transformation Detection Contributes to Screening of Behaviorally Active Compounds: Dynamic Binding Process Analysis of DhelOBP21 from Dastarcus helophoroides.Journal of chemical ecology · 2017Article
- Selectivity and ligand-based molecular modeling of an odorant-binding protein from the leaf beetle Ambrostoma quadriimpressum (Coleoptera: Chrysomelidae) in relation to habitat-related volatiles.Scientific reports · 2017Article
- Structural Basis of Alcohol Inhibition of the Pentameric Ligand-Gated Ion Channel ELIC.Structure (London, England : 1993) · 2017Article
- Key Odorants Regulate Food Attraction inFrontiers in behavioral neuroscience · 2017Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
It is now generally accepted that many of the physiological effects of alcohol consumption are a direct result of binding to specific sites in neuronal proteins such as ion channels or other components of neuronal signaling cascades. Binding to these targets generally occurs in water-filled pockets and leads to alterations in protein structure and dynamics. However, the precise interactions required to confer alcohol sensitivity to a particular protein remain undefined. Using information from the previously solved crystal structures of the Drosophila melanogaster protein LUSH in complexes with short-chain alcohols, we have designed and tested the effects of specific amino acid substitutions on alcohol binding. The effects of these substitutions, specifically S52A, T57S, and T57A, were examined using a combination of molecular dynamics, X-ray crystallography, fluorescence spectroscopy, and thermal unfolding. These studies reveal that the binding of ethanol is highly sensitive to small changes in the composition of the alcohol binding site. We find that T57 is the most critical residue for binding alcohols; the T57A substitution completely abolishes binding, while the T57S substitution differentially affects ethanol binding compared to longer-chain alcohols. The additional requirement for a potential hydrogen-bond acceptor at position 52 suggests that both the presence of multiple hydrogen-bonding groups and the identity of the hydrogen-bonding residues are critical for defining an ethanol binding site. These results provide new insights into the detailed chemistry of alcohol's interactions with proteins.
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Registered trials
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