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Conformational change of the rat odorant-binding protein OBP-1F upon odorant binding
, 2004 Nespoulous, Claude +4 more
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Odorant‐binding proteins of mammals
Biological Reviews, 2021ABSTRACTOdorant‐binding proteins (OBPs) of vertebrates belong to the lipocalin superfamily and perform a dual function: solubilizing and ferrying volatile pheromones to the olfactory receptors, and complexing the same molecules in specialized glands and assisting their release into the environment.
Paolo Pelosi, Wolfgang Knoll
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Mammalian odorant binding proteins
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000Odorant binding proteins (OBPs) pertain to one of the most abundant classes of proteins found in the olfactory apparatus. OBPs are a sub-class of lipocalins, defined by their property of reversibly binding volatile chemicals, that we call 'odorants'. Numerous sequences of OBPs are now available, derived from protein sequencing from nasal mucus material,
Tegoni, Mariella +7 more
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Odorant-binding proteins in insects
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 1995This paper reviews the characteristics of pheromone and odorant-binding proteins (OBP) in insects, with particular reference to Lepidoptera. They are small (15 kDa) soluble proteins, very concentrated in the lymph of chemosensory sensilla and belonging to two major classes, pheromone-binding proteins (PBP) and general odorant-binding proteins.
PELOSI, PAOLO, MAIDA R.
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Deswapping bovine odorant binding protein
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2008The X-ray structure of bovine Odorant Binding Protein (bOBP) revealed its association as a domain swapped dimer. bOBP, devoid of any cysteines, contrasts with other mammalian OBPs, which are monomeric and possess at least one disulfide bridge. We have produced a mutant of bOBP in which a glycine residue was inserted after position 121.
RAMONI, Roberto +6 more
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Critical Reviews in Biochemistry and Molecular Biology, 1994
Odorant-binding proteins (OBPs) are low-molecular-weight soluble proteins highly concentrated in the nasal mucus of vertebrates and in the sensillar lymph of insects. Their affinity toward odors and pheromones suggests a role in olfactory perception, but their physiological function has not been clearly defined.
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Odorant-binding proteins (OBPs) are low-molecular-weight soluble proteins highly concentrated in the nasal mucus of vertebrates and in the sensillar lymph of insects. Their affinity toward odors and pheromones suggests a role in olfactory perception, but their physiological function has not been clearly defined.
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Odorant-binding proteins of the mouse
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 1995After the isolation of two odorant-binding proteins (OBP-I and OBP-II) from mouse nasal tissue, we have purified two additional OBPs, which bind tritiated 2-isobutyl-3-methoxypyrazine. OBP-III is a homodimer with subunits of M(r) 22,000 and pI 4.2. OBP-IV is a homodimer with subunits of M(r) 21,000 and pI 4.85.
PES D, PELOSI, PAOLO
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Odorant‐Binding Proteins: Structural Aspects
Annals of the New York Academy of Sciences, 1998ABSTRACT: Structural data on odorant‐binding proteins (OBPs), both in vertebrates and in insects, are reviewed and discussed. OBPs are soluble proteins interacting with odor molecules and Pheromones in the perireceptor areas, the nasal mucus in vertebrates and the sensillar lymph in insects.
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Pesticide Biochemistry and Physiology, 2022
The Liriomyza trifolii is a highly invasive polyphagia pest. Understanding the physiological functions of odorant binding proteins (OBPs) in the chemical communication of L. trifolii can lead to effective pest management strategies. Seven full-length OBPs were identified by transcriptome screening of L. trifolii adults.
Qikai, Zhang +6 more
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The Liriomyza trifolii is a highly invasive polyphagia pest. Understanding the physiological functions of odorant binding proteins (OBPs) in the chemical communication of L. trifolii can lead to effective pest management strategies. Seven full-length OBPs were identified by transcriptome screening of L. trifolii adults.
Qikai, Zhang +6 more
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DyBOBS: A Dynamic Biomimetic Assay for Odorant-Binding to Odor-Binding Protein
Chemosensory Perception, 2010An in vitro system was developed to mimic the structural and flow conditions of the human olfactory epithelium and to measure the dynamics of odorant-binding to odor-binding protein (OBP). A hydrophilic fused silica capillary, coated internally with a thin (about 1.3 µm) aqueous film of recombinant rat-OBP3 mimicked the human olfactory epithelium ...
Yabuki, Masayuki +4 more
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