The structure of neuronal calcium sensor-1 in solution revealed by molecular dynamics simulations.

Neuronal calcium sensor-1 (NCS-1) is a protein able to trigger signal transduction processes by binding a large number of substrates and re-shaping its structure depending on the environmental conditions. The X-ray crystal structure of the unmyristoilated NCS-1 shows a large solvent-exposed hydropho...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Luca Bellucci, Stefano Corni, Rosa Di Felice, Emanuele Paci
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/e7bda8b952ef4a9caea312e2b367d63b
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:e7bda8b952ef4a9caea312e2b367d63b
record_format	dspace
spelling	oai:doaj.org-article:e7bda8b952ef4a9caea312e2b367d63b2021-11-18T08:53:05ZThe structure of neuronal calcium sensor-1 in solution revealed by molecular dynamics simulations.1932-620310.1371/journal.pone.0074383https://doaj.org/article/e7bda8b952ef4a9caea312e2b367d63b2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24098643/?tool=EBIhttps://doaj.org/toc/1932-6203Neuronal calcium sensor-1 (NCS-1) is a protein able to trigger signal transduction processes by binding a large number of substrates and re-shaping its structure depending on the environmental conditions. The X-ray crystal structure of the unmyristoilated NCS-1 shows a large solvent-exposed hydrophobic crevice (HC); this HC is partially occupied by the C-terminal tail and thus elusive to the surrounding solvent. We studied the native state of NCS-1 by performing room temperature molecular dynamics (MD) simulations starting from the crystal and the solution structures. We observe relaxation to a state independent of the initial structure, in which the C-terminal tail occupies the HC. We suggest that the C-terminal tail shields the HC binding pocket and modulates the affinity of NCS-1 for its natural targets. By analyzing the topology and nature of the inter-residue potential energy, we provide a compelling description of the interaction network that determines the three-dimensional organization of NCS-1.Luca BellucciStefano CorniRosa Di FeliceEmanuele PaciPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 9, p e74383 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Luca Bellucci Stefano Corni Rosa Di Felice Emanuele Paci The structure of neuronal calcium sensor-1 in solution revealed by molecular dynamics simulations.
description	Neuronal calcium sensor-1 (NCS-1) is a protein able to trigger signal transduction processes by binding a large number of substrates and re-shaping its structure depending on the environmental conditions. The X-ray crystal structure of the unmyristoilated NCS-1 shows a large solvent-exposed hydrophobic crevice (HC); this HC is partially occupied by the C-terminal tail and thus elusive to the surrounding solvent. We studied the native state of NCS-1 by performing room temperature molecular dynamics (MD) simulations starting from the crystal and the solution structures. We observe relaxation to a state independent of the initial structure, in which the C-terminal tail occupies the HC. We suggest that the C-terminal tail shields the HC binding pocket and modulates the affinity of NCS-1 for its natural targets. By analyzing the topology and nature of the inter-residue potential energy, we provide a compelling description of the interaction network that determines the three-dimensional organization of NCS-1.
format	article
author	Luca Bellucci Stefano Corni Rosa Di Felice Emanuele Paci
author_facet	Luca Bellucci Stefano Corni Rosa Di Felice Emanuele Paci
author_sort	Luca Bellucci
title	The structure of neuronal calcium sensor-1 in solution revealed by molecular dynamics simulations.
title_short	The structure of neuronal calcium sensor-1 in solution revealed by molecular dynamics simulations.
title_full	The structure of neuronal calcium sensor-1 in solution revealed by molecular dynamics simulations.
title_fullStr	The structure of neuronal calcium sensor-1 in solution revealed by molecular dynamics simulations.
title_full_unstemmed	The structure of neuronal calcium sensor-1 in solution revealed by molecular dynamics simulations.
title_sort	structure of neuronal calcium sensor-1 in solution revealed by molecular dynamics simulations.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/e7bda8b952ef4a9caea312e2b367d63b
work_keys_str_mv	AT lucabellucci thestructureofneuronalcalciumsensor1insolutionrevealedbymoleculardynamicssimulations AT stefanocorni thestructureofneuronalcalciumsensor1insolutionrevealedbymoleculardynamicssimulations AT rosadifelice thestructureofneuronalcalciumsensor1insolutionrevealedbymoleculardynamicssimulations AT emanuelepaci thestructureofneuronalcalciumsensor1insolutionrevealedbymoleculardynamicssimulations AT lucabellucci structureofneuronalcalciumsensor1insolutionrevealedbymoleculardynamicssimulations AT stefanocorni structureofneuronalcalciumsensor1insolutionrevealedbymoleculardynamicssimulations AT rosadifelice structureofneuronalcalciumsensor1insolutionrevealedbymoleculardynamicssimulations AT emanuelepaci structureofneuronalcalciumsensor1insolutionrevealedbymoleculardynamicssimulations
_version_	1718421235067518976

The structure of neuronal calcium sensor-1 in solution revealed by molecular dynamics simulations.

Ejemplares similares