The Dynamic Behavior of the P2X4 Ion Channel in the Closed Conformation

We present the results of a detailed molecular dynamics study of the closed form of the P2X4 receptor. The fluctuations observed in the simulations were compared with the changes that occur in the transition from the closed to the open structure. To get further insight on the opening mechanism, the...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Pierdominici-Sottile, G., Moffatt, L., Palma, J.
Formato:	JOUR
Materias:	purinergic P2X4 receptor channel gating chemistry metabolism molecular dynamics protein conformation Ion Channel Gating Molecular Dynamics Simulation Protein Conformation Receptors, Purinergic P2X4
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_00063495_v111_n12_p2642_PierdominiciSottile
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_00063495_v111_n12_p2642_PierdominiciSottile
record_format	dspace
spelling	todo:paper_00063495_v111_n12_p2642_PierdominiciSottile2023-10-03T14:05:05Z The Dynamic Behavior of the P2X4 Ion Channel in the Closed Conformation Pierdominici-Sottile, G. Moffatt, L. Palma, J. purinergic P2X4 receptor channel gating chemistry metabolism molecular dynamics protein conformation Ion Channel Gating Molecular Dynamics Simulation Protein Conformation Receptors, Purinergic P2X4 We present the results of a detailed molecular dynamics study of the closed form of the P2X4 receptor. The fluctuations observed in the simulations were compared with the changes that occur in the transition from the closed to the open structure. To get further insight on the opening mechanism, the actual displacements were decomposed into interchain motions and intrachain deformations. This analysis revealed that the iris-like expansion of the transmembrane helices mainly results from interchain motions that already take place in the closed conformation. However, these movements cannot reach the amplitude required for the opening of the channel because they are impeded by interactions occurring around the ATP binding pocket. This suggests that the union of ATP produces distortions in the chains that eliminate the restrictions on the interchain displacements, leading to the opening of the pore. © 2016 Biophysical Society Fil:Moffatt, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00063495_v111_n12_p2642_PierdominiciSottile
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	purinergic P2X4 receptor channel gating chemistry metabolism molecular dynamics protein conformation Ion Channel Gating Molecular Dynamics Simulation Protein Conformation Receptors, Purinergic P2X4
spellingShingle	purinergic P2X4 receptor channel gating chemistry metabolism molecular dynamics protein conformation Ion Channel Gating Molecular Dynamics Simulation Protein Conformation Receptors, Purinergic P2X4 Pierdominici-Sottile, G. Moffatt, L. Palma, J. The Dynamic Behavior of the P2X4 Ion Channel in the Closed Conformation
topic_facet	purinergic P2X4 receptor channel gating chemistry metabolism molecular dynamics protein conformation Ion Channel Gating Molecular Dynamics Simulation Protein Conformation Receptors, Purinergic P2X4
description	We present the results of a detailed molecular dynamics study of the closed form of the P2X4 receptor. The fluctuations observed in the simulations were compared with the changes that occur in the transition from the closed to the open structure. To get further insight on the opening mechanism, the actual displacements were decomposed into interchain motions and intrachain deformations. This analysis revealed that the iris-like expansion of the transmembrane helices mainly results from interchain motions that already take place in the closed conformation. However, these movements cannot reach the amplitude required for the opening of the channel because they are impeded by interactions occurring around the ATP binding pocket. This suggests that the union of ATP produces distortions in the chains that eliminate the restrictions on the interchain displacements, leading to the opening of the pore. © 2016 Biophysical Society
format	JOUR
author	Pierdominici-Sottile, G. Moffatt, L. Palma, J.
author_facet	Pierdominici-Sottile, G. Moffatt, L. Palma, J.
author_sort	Pierdominici-Sottile, G.
title	The Dynamic Behavior of the P2X4 Ion Channel in the Closed Conformation
title_short	The Dynamic Behavior of the P2X4 Ion Channel in the Closed Conformation
title_full	The Dynamic Behavior of the P2X4 Ion Channel in the Closed Conformation
title_fullStr	The Dynamic Behavior of the P2X4 Ion Channel in the Closed Conformation
title_full_unstemmed	The Dynamic Behavior of the P2X4 Ion Channel in the Closed Conformation
title_sort	dynamic behavior of the p2x4 ion channel in the closed conformation
url	http://hdl.handle.net/20.500.12110/paper_00063495_v111_n12_p2642_PierdominiciSottile
work_keys_str_mv	AT pierdominicisottileg thedynamicbehaviorofthep2x4ionchannelintheclosedconformation AT moffattl thedynamicbehaviorofthep2x4ionchannelintheclosedconformation AT palmaj thedynamicbehaviorofthep2x4ionchannelintheclosedconformation AT pierdominicisottileg dynamicbehaviorofthep2x4ionchannelintheclosedconformation AT moffattl dynamicbehaviorofthep2x4ionchannelintheclosedconformation AT palmaj dynamicbehaviorofthep2x4ionchannelintheclosedconformation
_version_	1782027846844153856

The Dynamic Behavior of the P2X4 Ion Channel in the Closed Conformation

Ejemplares similares