Odorant binding and conformational dynamics in the odorant binding protein
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...
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ftinraparis:oai:prodinra.inra.fr:10138 2023-05-15T18:05:20+02:00 Odorant binding and conformational dynamics in the odorant binding protein Hajjar, Eric Perahia, David Debat, Helene Nespoulous, Claude Robert, Charles H. 2006 application/pdf http://prodinra.inra.fr/ft/234630F2-78A0-4B1B-96ED-86739843A5E8 http://prodinra.inra.fr/record/10138 https://doi.org/10.1074/jbc.M604869200 eng eng http://creativecommons.org/licenses/by-nd-nc/1.0/ CC-BY-ND-NC Journal of Biological Chemistry 40 (281), 29929-29937. (2006) ODORANT BINDING PROTEIN;RAT rattus rattus porc sus scrofa épithélium olfactif olfaction odorat protéine thymol ARTICLE 2006 ftinraparis https://doi.org/10.1074/jbc.M604869200 2015-10-30T07:45:55Z 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. Article in Journal/Newspaper Rattus rattus Institut National de la Recherche Agronomique: ProdINRA Journal of Biological Chemistry 281 40 29929 29937 |
institution |
Open Polar |
collection |
Institut National de la Recherche Agronomique: ProdINRA |
op_collection_id |
ftinraparis |
language |
English |
topic |
ODORANT BINDING PROTEIN;RAT rattus rattus porc sus scrofa épithélium olfactif olfaction odorat protéine thymol |
spellingShingle |
ODORANT BINDING PROTEIN;RAT rattus rattus porc sus scrofa épithélium olfactif olfaction odorat protéine thymol Hajjar, Eric Perahia, David Debat, Helene Nespoulous, Claude Robert, Charles H. Odorant binding and conformational dynamics in the odorant binding protein |
topic_facet |
ODORANT BINDING PROTEIN;RAT rattus rattus porc sus scrofa épithélium olfactif olfaction odorat protéine thymol |
description |
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. |
format |
Article in Journal/Newspaper |
author |
Hajjar, Eric Perahia, David Debat, Helene Nespoulous, Claude Robert, Charles H. |
author_facet |
Hajjar, Eric Perahia, David Debat, Helene Nespoulous, Claude Robert, Charles H. |
author_sort |
Hajjar, Eric |
title |
Odorant binding and conformational dynamics in the odorant binding protein |
title_short |
Odorant binding and conformational dynamics in the odorant binding protein |
title_full |
Odorant binding and conformational dynamics in the odorant binding protein |
title_fullStr |
Odorant binding and conformational dynamics in the odorant binding protein |
title_full_unstemmed |
Odorant binding and conformational dynamics in the odorant binding protein |
title_sort |
odorant binding and conformational dynamics in the odorant binding protein |
publishDate |
2006 |
url |
http://prodinra.inra.fr/ft/234630F2-78A0-4B1B-96ED-86739843A5E8 http://prodinra.inra.fr/record/10138 https://doi.org/10.1074/jbc.M604869200 |
genre |
Rattus rattus |
genre_facet |
Rattus rattus |
op_source |
Journal of Biological Chemistry 40 (281), 29929-29937. (2006) |
op_rights |
http://creativecommons.org/licenses/by-nd-nc/1.0/ |
op_rightsnorm |
CC-BY-ND-NC |
op_doi |
https://doi.org/10.1074/jbc.M604869200 |
container_title |
Journal of Biological Chemistry |
container_volume |
281 |
container_issue |
40 |
container_start_page |
29929 |
op_container_end_page |
29937 |
_version_ |
1766176801105641472 |