Résumé
| langue originale | Anglais |
|---|---|
| titre | Abstracts of the 255th Annual Meeting and Exposition of the American Chemical Society |
| Editeur | ACS |
| état | Publié - 2018 |
| Evénement | 255th ACS National Meeting & Exposition - New Orleans, LA, États-Unis Durée: 18 mars 2018 → 22 mars 2018 |
Réunion
| Réunion | 255th ACS National Meeting & Exposition |
|---|---|
| Pays | États-Unis |
| La ville | New Orleans, LA |
| période | 18/03/18 → 22/03/18 |
Empreinte digitale
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Intrinsic Flexibility of the μ Opioid Receptor through Multiscale Modelling Approaches - COMP403. / Vercauteren, Daniel; Fossepre, Mathieu; Leherte, Laurence; Laaksonen, Aatto.
Abstracts of the 255th Annual Meeting and Exposition of the American Chemical Society. ACS, 2018.Résultats de recherche: Contribution dans un livre/un catalogue/un rapport/dans les actes d'une conférence › Article dans les actes d'une conférence/un colloque
TY - GEN
T1 - Intrinsic Flexibility of the μ Opioid Receptor through Multiscale Modelling Approaches - COMP403
AU - Vercauteren, Daniel
AU - Fossepre, Mathieu
AU - Leherte, Laurence
AU - Laaksonen, Aatto
PY - 2018
Y1 - 2018
N2 - Recent releases of numerous G protein-coupled receptors crystalline structures created the opportunity for computational methods to widely explore their dynamics. Here, we study the biological implication of the intrinsic flexibility properties of µ opioid receptor (µOR). First, one performed classical all-atom (AA) Molecular Dynamics (MD) simulations of µOR in its apo-form. We highlighted that the various degrees of bendability of the α-helices present important consequences on the plasticity of the µOR binding site. Hence, this latter adopts a wide diversity of shape and volume, explaining why µOR interacts with very diverse ligands. Then, one introduces a new strategy for parameterizing purely mechanical but precise coarse-grained (CG) elastic network models (ENMs). Those CG ENMs reproduced in a high accurate way the flexibility properties of µOR as observed with the AA simulations. At last, ones uses network modularization to design multi-grained (MG) models. They represent a novel type of low resolution models, different in nature versus CG models as being true multi-resolution models, i.e., each MG grouping a different number of residues. The three parts of our work constitute an integrated hierarchical and multiscale approach for tackling the flexibility of µOR.
AB - Recent releases of numerous G protein-coupled receptors crystalline structures created the opportunity for computational methods to widely explore their dynamics. Here, we study the biological implication of the intrinsic flexibility properties of µ opioid receptor (µOR). First, one performed classical all-atom (AA) Molecular Dynamics (MD) simulations of µOR in its apo-form. We highlighted that the various degrees of bendability of the α-helices present important consequences on the plasticity of the µOR binding site. Hence, this latter adopts a wide diversity of shape and volume, explaining why µOR interacts with very diverse ligands. Then, one introduces a new strategy for parameterizing purely mechanical but precise coarse-grained (CG) elastic network models (ENMs). Those CG ENMs reproduced in a high accurate way the flexibility properties of µOR as observed with the AA simulations. At last, ones uses network modularization to design multi-grained (MG) models. They represent a novel type of low resolution models, different in nature versus CG models as being true multi-resolution models, i.e., each MG grouping a different number of residues. The three parts of our work constitute an integrated hierarchical and multiscale approach for tackling the flexibility of µOR.
M3 - Conference contribution
BT - Abstracts of the 255th Annual Meeting and Exposition of the American Chemical Society
PB - ACS
ER -