0000000000338379

AUTHOR

Antoni J. Borysik

showing 2 related works from this author

Structure of rat odorant-binding protein OBP1 at 1.6 angstrom resolution

2009

The nasal mucosa is a specialist interfacial region sandwiched between the olfactory system and the gaseous chemical milieu. In mammals and insects, this region is rich in odorant-binding proteins that are thought to aid olfaction by assisting mass transfer of the many different organoleptic compounds that make up the olfactory landscape. However, in mammals at least, our grasp on the exact function of odorant-binding proteins is tentative and better insight into the role of these proteins is warranted, not least because of their apparent significance in the olfactory systems of insects. Here, the crystal structure of rat odorant-binding protein 1 is reported at 1.6 Å resolution. This prote…

Models MolecularOlfactory systemCristallographyProtein ConformationRecombinant Fusion ProteinsMolecular Sequence DataOlfactionOBP1Crystallography X-RayReceptors Odorant010402 general chemistry01 natural sciencesPheromonesPichia pastoris03 medical and health sciences[ CHIM.CRIS ] Chemical Sciences/CristallographyProtein structureSpecies SpecificityStructural BiologyODORANT-BINDING PROTEINS[CHIM.CRIS]Chemical Sciences/CristallographyAnimalsAmino Acid SequencePeptide sequence030304 developmental biology0303 health sciencesBinding SitesSequence Homology Amino AcidbiologyProteinsGeneral MedicineLigand (biochemistry)biology.organism_classificationLipocalinsRatsCristallographie0104 chemical sciencesTransport proteinDNA-Binding ProteinsBiochemistryOdorant-binding proteinbiology.proteinODORANT-BINDING PROTEINS;OBP1Sequence Alignment
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Rapid odorant release in mammalian odour binding proteins facilitates their temporal coupling to odorant signals.

2010

 ; We have measured the effect of rat odorant-binding protein 1 on the rates of ligand uptake and liquid-to-air transfer rates with a set of defined odorous compounds. Comparison of observed rate constants (k(obs)) with data simulated over a wide range of different kinetic and thermodynamic regimes shows that the data do not agree with the previously held view of a slow off-rate regime (k(off) <0.0004 s(-1)). We propose that a rapid koff would be a necessary requirement for such a system, since slow odorant-release rates would result in significant decorrelation between the olfactory world and odour perception. (c) 2010 Elsevier Ltd. All rights reserved.

[SDV.BIO]Life Sciences [q-bio]/BiotechnologyKineticsAnalytical chemistryOlfactionAcetatesCalorimetryIn Vitro Techniques[ SDV.BA ] Life Sciences [q-bio]/Animal biologyLigandsReceptors OdorantDNA-binding proteinMass Spectrometry03 medical and health sciences0302 clinical medicineReaction rate constantStructural BiologyODORANT-BINDING PROTEINSAnimals[INFO.INFO-BT]Computer Science [cs]/BiotechnologyMolecular Biology030304 developmental biology0303 health sciencesChemistryTemporal couplingLigand[SDV.BA]Life Sciences [q-bio]/Animal biology[ SDV.BIO ] Life Sciences [q-bio]/BiotechnologyRecombinant ProteinsRatsSmellKineticsOdorantsBiophysicsOLFACTIONThermodynamics[ INFO.INFO-BT ] Computer Science [cs]/Biotechnology030217 neurology & neurosurgerypsychological phenomena and processesSignal TransductionJournal of molecular biology
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