Artículo
Magnesium interactions with a CX26 connexon in lipid bilayers
Fecha de publicación:
20/07/2019
Editorial:
Springer Verlag Berlín
Revista:
Journal of Molecular Modeling
ISSN:
1610-2940
e-ISSN:
0948-5023
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
Following our previous work, where we described the interaction of calcium with the Cx26 hemichannel, we further explore the same system by atomistic molecular dynamics simulations considering a different di-cation, magnesium. Specifically, the interaction of magnesium di-cation with the previously reported calcium binding sites (ASP2, ASP117, ASP159, GLU114, GLU119, GLU120, and VAL226) was investigated to identify similarities and differences between them. In order to do so, four extensive simulations were carried out. Two of them considered a Cx26 hemichannel embedded on a POPC bilayer with one of the di-cations and a sodium-chlorine solution. For the remaining two, no di-cations were included and a sodium-chlorine or potassium-chlorine solution was considered. Potassium has a similar atomic mass to calcium, and sodium to magnesium, but they both differ in charge (1e and 2e respectively). Magnesium and calcium, even having the same charge, showed different affinity for the explored protein. From the calcium binding sites referred above, we found that the magnesium di-cations only binds strongly to the GLU114 site of one connexin. For the sodium and potassium simulations, no specific interactions with the protein were found. Altogether, these results suggest that mass and steric effects play an important role in determining cation binding to Cx26 hemichannels.
Palabras clave:
CALCIUM
,
CONNEXINS
,
CX26
,
LIPID BILAYER
,
MAGNESIUM
,
MOLECULAR DYNAMICS
Archivos asociados
Licencia
Identificadores
Colecciones
Articulos(IFIBA)
Articulos de INST.DE FISICA DE BUENOS AIRES
Articulos de INST.DE FISICA DE BUENOS AIRES
Citación
Albano, Juan Manuel Ricardo; Facelli, Julio C.; Ferraro, Marta Beatriz; Pickholz, Mónica Andrea; Magnesium interactions with a CX26 connexon in lipid bilayers; Springer Verlag Berlín; Journal of Molecular Modeling; 25; 8; 20-7-2019; 1-8
Compartir
Altmétricas