ArticleInternational journal of biological sciences2015
Structure-Based Analysis of the Ligand-Binding Mechanism for DhelOBP21, a C-minus Odorant Binding Protein, from Dastarcus helophoroides (Fairmaire; Coleoptera: Bothrideridae).
Article in International journal of biological sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 48 citations in OpenAlex.
- Molecular Recognition Mechanism of Key VOCs by Odorant-Binding Proteins in the Western Corn Rootworm (Insects · 2026Article
- Prokaryotic Expression and Binding Characteristics of Odor-Binding Protein GqinOBP10 inInternational journal of molecular sciences · 2025Article
- The Odorant-Binding Proteins AspiOBP1 and AspiOBP2 inInternational journal of molecular sciences · 2025Article
- Molecular characterization of a Minus-C odorant-binding protein fromFrontiers in physiology · 2025Article
- Genetic Structure ofEcology and evolution · 2024Article
- Revealing the pH-dependent conformational changes in sol g 2.1 protein and potential ligands binding.Scientific reports · 2024Article
- Ligand-binding properties of XaffOBP9, a Minus-C odorant-binding protein fromFrontiers in physiology · 2023Article
- Roles of insect odorant binding proteins in communication and xenobiotic adaptation.Frontiers in insect science · 2023Review
- Characterizations of botanical attractant of Halyomorpha halys and selection of relevant deorphanization candidates via computational approach.Scientific reports · 2022Article
- A Salivary Odorant-Binding Protein MediatesInternational journal of molecular sciences · 2021Article
- Antennal Enriched Odorant Binding Proteins Are Required for Odor Communication inBiomolecules · 2021Article
- Identification and Functional Analysis of SlitOBP11 FromFrontiers in physiology · 2021Article
- Identification and motif analyses of candidate nonreceptor olfactory genes of Dendroctonus adjunctus Blandford (Coleoptera: Curculionidae) from the head transcriptome.Scientific reports · 2020Article
- Characterization of MaltOBP1, a Minus-C Odorant-Binding Protein, From the Japanese Pine Sawyer Beetle,Frontiers in physiology · 2020Article
- Functional Analysis of Two Odorant-Binding Proteins, MaltOBP9 and MaltOBP10, inFrontiers in physiology · 2020Article
- Deciphering the Odorant Binding, Activation, and Discrimination Mechanism of Dhelobp21 from Dastarus Helophoroides.Scientific reports · 2018Article
- Insights from the Molecular modeling, docking analysis of illicit drugs and Bomb Compounds with Honey Bee Odorant Binding Proteins (OBPs).Bioinformation · 2018Article
- Two Odorant-Binding Proteins of the Dark Black Chafer (Frontiers in physiology · 2018Article
- Odorant Receptors and Odorant-Binding Proteins as Insect Pest Control Targets: A Comparative Analysis.Frontiers in physiology · 2018Review
- Structural Transformation Detection Contributes to Screening of Behaviorally Active Compounds: Dynamic Binding Process Analysis of DhelOBP21 from Dastarcus helophoroides.Journal of chemical ecology · 2017Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Odorant binding proteins (OBPs) transport hydrophobic odor molecules across the sensillar lymph to trigger a neuronal response. Herein, the Minus-C OBP (DhelOBP21) was characterized from Dastarcus helophoroides, the most important natural parasitic enemy insect that targets Monochamus alternatus. Homology modeling and molecular docking were conducted on the interaction between DhelOBP21 and 17 volatile molecules (including volatiles from pine bark, the larva of M. alternatus, and the faeces of the larva). The predicted three-dimensional structure showed only two disulfide bridges and a hydrophobic binding cavity with a short C-terminus. Ligand-binding experiments using N-phenylnaphthylamine (1-NPN) as a fluorescent probe showed that DhelOBP21 exhibited better binding affinities against those ligands with a molecular volume between 100 and 125 Å(³) compared with ligands with a molecular volume between 160 and 185 Å(³). Molecules that are too big or too small are not conducive for binding. We mutated the amino acid residues of the binding cavity to increase either hydrophobicity or hydrophilia. Ligand-binding experiments and cyber molecular docking assays indicated that hydrophobic interactions are more significant than hydrogen-bonding interactions. Although hydrogen-bond interactions could be predicted for some binding complexes, the hydrophobic interactions had more influence on binding following hydrophobic changes that affected the cavity. The orientation of ligands affects binding by influencing hydrophobic interactions. The binding process is controlled by multiple factors. This study provides a basis to explore the ligand-binding mechanisms of Minus-C OBP.
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