Odorant Binding and Conformational Dynamics in the Odorant-binding Protein*
By Eric Hajjar, D. Pérahia, H. Débat, C. Nespoulous, C. Robert. 2006
61 citations recorded by the source corpus.
In mammals, the olfactory epithelium secretes odorant-binding proteins (OBPs), which are lipocalins found freely dissolved in the mucus layer protecting the olfactory neurons. OBPs may act as passive transporters of predominantly hydrophobic odorant molecules across the aqueous mucus layer, or they may play a more active role in which the olfactory neuronal receptor recognizes the OBP-ligand complex. To better understand the molecular events accompanying the initial steps in the olfaction process, we have performed molecular dynamics studies of rat and pig OBPs with the odorant molecule thymol. These calculations provide an atomic level description of conformational changes and pathway intermediates that remain difficult to study directly. A series of eight independent molecular dynamics trajectories of rat OBP permitted the observation of a consensus pathway for ligand unbinding and the calculation of the potential of mean force (PMF) along this path. Titration microcalorimetry confirmed the specific binding of thymol to this protein with a strong hydrophobic component. In both rat and pig OBPs we observed lipocalin strand pair opening in the presence of ligand, consistent with potential roles of these proteins in olfactive receptor recognition.
Subfields: Cellular and Molecular Neuroscience, Nutrition and Dietetics, Sensory Systems
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Citations in the corpus
- Phenylalanine 35 and tyrosine 82 are involved in the uptake and release of ligand by porcine odorant-binding protein. (2009, background): “for thymol [28], the hereby artificially accelerated UND dissociation pathway (300–500 ps) takes place along the axis between the D and E strands but not between these two strands leading to the important participation of the Tyr82, Phe66 and Pro34 residues, the aldehyde hydrogen of the undecanal li”