ArticleProtein science : a publication of the Protein Society2013
A novel mechanism of ligand binding and release in the odorant binding protein 20 from the malaria mosquito Anopheles gambiae.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 32 citations in OpenAlex.
- VOCs Profiling and Quality Assessment of Milk Employing Odorant-Binding Proteins-Based Fluorescence Biosensor.International journal of molecular sciences · 2026Article
- A Deeper Insight into the Tick Salivary Protein Families under the Light of Alphafold2 and Dali: Introducing the TickSialoFam 2.0 Database.International journal of molecular sciences · 2022Article
- Review
- The Drosophila odorant-binding protein 28a is involved in the detection of the floral odour ß-ionone.Cellular and molecular life sciences : CMLS · 2020Article
- A subset of chemosensory genes differs between two populations of a specialized leaf beetle after host plant shift.Ecology and evolution · 2018Article
- New insights on repellent recognition by Anopheles gambiae odorant-binding protein 1.PloS one · 2018Article
- A Synergistic Transcriptional Regulation of Olfactory Genes Drives Blood-Feeding Associated Complex Behavioral Responses in the MosquitoFrontiers in physiology · 2018Article
- Structural Transformation Detection Contributes to Screening of Behaviorally Active Compounds: Dynamic Binding Process Analysis of DhelOBP21 from Dastarcus helophoroides.Journal of chemical ecology · 2017Article
- Article
- Multiple Binding Poses in the Hydrophobic Cavity of Bee Odorant Binding Protein AmelOBP14.Journal of chemical information and modeling · 2015Article
- Structure-Based Analysis of the Ligand-Binding Mechanism for DhelOBP21, a C-minus Odorant Binding Protein, from Dastarcus helophoroides (Fairmaire; Coleoptera: Bothrideridae).International journal of biological sciences · 2015Article
- Protein science "best paper" awards to Mark Landau and Brian Ziemba.Protein science : a publication of the Protein Society · 2014Article
- Crystal and solution studies of the "Plus-C" odorant-binding protein 48 from Anopheles gambiae: control of binding specificity through three-dimensional domain swapping.The Journal of biological chemistry · 2013Article
- Interactions of Anopheles gambiae odorant-binding proteins with a human-derived repellent: implications for the mode of action of n,n-diethyl-3-methylbenzamide (DEET).The Journal of biological chemistry · 2013Article
- Potential cooperations between odorant-binding proteins of the scarab beetle Holotrichia oblita Faldermann (Coleoptera: Scarabaeidae).PloS one · 2013Article
- Article
- Daily rhythms in antennal protein and olfactory sensitivity in the malaria mosquito Anopheles gambiae.Scientific reports · 2013Article
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4 authors at 1 institution in 1 country.
Funding
Abstract
Anopheles gambiae mosquitoes that transmit malaria are attracted to humans by the odor molecules that emanate from skin and sweat. Odorant binding proteins (OBPs) are the first component of the olfactory apparatus to interact with odorant molecules, and so present potential targets for preventing transmission of malaria by disrupting the normal olfactory responses of the insect. AgamOBP20 is one of a limited subset of OBPs that it is preferentially expressed in female mosquitoes and its expression is regulated by blood feeding and by the day/night light cycles that correlate with blood-feeding behavior. Analysis of AgamOBP20 in solution reveals that the apo-protein exhibits significant conformational heterogeneity but the binding of odorant molecules results in a significant conformational change, which is accompanied by a reduction in the conformational flexibility present in the protein. Crystal structures of the free and bound states reveal a novel pathway for entrance and exit of odorant molecules into the central-binding pocket, and that the conformational changes associated with ligand binding are a result of rigid body domain motions in α-helices 1, 4, and 5, which act as lids to the binding pocket. These structures provide new insights into the specific residues involved in the conformational adaptation to different odorants and have important implications in the selection and development of reagents targeted at disrupting normal OBP function.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.