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« Previous AbstractRole of sex pheromone components in behavioral reproductive isolation betweenAutographa gamma (L.) and eitherTrichoplusia ni (Hubner) ORChrysodeixis chalcites (Esp.) (Lepidoptera: Noctuidae: Plusiinae)    Next AbstractPheromone Perception: Mechanism of the Reversible Coil-Helix Transition in Antheraea polyphemus Pheromone-Binding Protein 1 »

Sci Rep


Title:Structure and Function Studies of Asian Corn Borer Ostrinia furnacalis Pheromone Binding Protein2
Author(s):Mazumder S; Dahal SR; Chaudhary BP; Mohanty S;
Address:"Department of Chemistry, Oklahoma State University, Stillwater, OK, 74078, USA. Department of Chemistry, Oklahoma State University, Stillwater, OK, 74078, USA. smita.mohanty@okstate.edu"
Journal Title:Sci Rep
Year:2018
Volume:20181120
Issue:1
Page Number:17105 -
DOI: 10.1038/s41598-018-35509-x
ISSN/ISBN:2045-2322 (Electronic) 2045-2322 (Linking)
Abstract:"Lepidopteran male moths have an extraordinarily sensitive olfactory system that is capable of detecting and responding to minute amounts of female-secreted pheromones over great distances. Pheromone-binding proteins (PBPs) in male antennae ferry the hydrophobic ligand across the aqueous lymph to the olfactory receptor neuron triggering the response. PBPs bind ligands at physiological pH of the lymph and release them at acidic pH near the receptor while undergoing a conformational change. In Anthereae polyphemus PBP1, ligand binding to the hydrophobic pocket and its release is regulated by two biological gates: His70 and His95 at one end of the pocket and C-terminus tail at the other end. Interestingly, in Asian corn borer Ostrinia furnacalis PBP2 (OfurPBP2), critical residues for ligand binding and release are substituted in both biological gates. The impact of these substitutions on the ligand binding and release mechanism in OfurPBP2 is not known. We report here overexpression of soluble OfurPBP2 and structural characterization at high and low pH by circular dichroism (CD) and NMR. Ligand binding and ab initio model development were carried out with fluorescence and small-angle X-ray scattering (SAXS) respectively. OfurPBP2 in solution at pH 6.5 is homogeneous, well-folded and has a compact globular shape"
Keywords:"Amino Acid Sequence Animals Carrier Proteins/*chemistry/genetics/*metabolism Insect Proteins/*chemistry/genetics/*metabolism Models, Molecular Moths Pheromones/*metabolism Protein Conformation Sequence Homology Structure-Activity Relationship;"
Notes:"MedlineMazumder, Suman Dahal, Salik R Chaudhary, Bharat P Mohanty, Smita eng 2011-65503-23501/USDA | National Institute of Food and Agriculture (NIFA)/International 1807722/National Science Foundation (NSF)/International Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. England 2018/11/22 Sci Rep. 2018 Nov 20; 8(1):17105. doi: 10.1038/s41598-018-35509-x"

 
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Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
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