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dc.contributor.author
Albano, Juan Manuel Ricardo
dc.contributor.author
Facelli, Julio C.
dc.contributor.author
Ferraro, Marta Beatriz
dc.contributor.author
Pickholz, Mónica Andrea
dc.date.available
2021-12-03T20:04:05Z
dc.date.issued
2019-07-20
dc.identifier.citation
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
dc.identifier.issn
1610-2940
dc.identifier.uri
http://hdl.handle.net/11336/148189
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer Verlag Berlín
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
CALCIUM
dc.subject
CONNEXINS
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CX26
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LIPID BILAYER
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MAGNESIUM
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MOLECULAR DYNAMICS
dc.subject.classification
Biofísica
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Magnesium interactions with a CX26 connexon in lipid bilayers
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2020-11-20T15:59:31Z
dc.identifier.eissn
0948-5023
dc.journal.volume
25
dc.journal.number
8
dc.journal.pagination
1-8
dc.journal.pais
Alemania
dc.journal.ciudad
Berlin
dc.description.fil
Fil: Albano, Juan Manuel Ricardo. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Física de Buenos Aires. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Física de Buenos Aires; Argentina
dc.description.fil
Fil: Facelli, Julio C.. University of Utah; Estados Unidos
dc.description.fil
Fil: Ferraro, Marta Beatriz. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Física de Buenos Aires. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Física de Buenos Aires; Argentina
dc.description.fil
Fil: Pickholz, Mónica Andrea. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Física de Buenos Aires. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Física de Buenos Aires; Argentina
dc.journal.title
Journal of Molecular Modeling
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs00894-019-4121-5
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s00894-019-4121-5
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