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dc.contributor.author
Bustos, Diego Martin
dc.contributor.author
Iglesias, Alberto Alvaro
dc.date.available
2019-12-27T02:51:03Z
dc.date.issued
2005-06
dc.identifier.citation
Bustos, Diego Martin; Iglesias, Alberto Alvaro; A model for the interaction between plant GAPN and 14-3-3ζ using protein-protein docking calculations, electrostatic potentials and kinetics; Elsevier Science Inc; Journal Of Molecular Graphics & Modelling; 23; 6; 6-2005; 490-502
dc.identifier.issn
1093-3263
dc.identifier.uri
http://hdl.handle.net/11336/93017
dc.description.abstract
Phosphorylated non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.9; GAPN) found in heterotrophic cells of wheat is activated by MgCl2. The divalent cation disrupts the interaction between GAPN and a 14-3-3 regulatory protein. This effect is quite remarkable, since it has previously been shown that 14-3-3 binding to a target protein requires divalent cations as Mg2+ or Ca2+. Binding of the divalent cation to 14-3-3 causes an increase in surface hydrophobicity. Crystal structure of a 14-3-3-target protein complex has been only determined for serotinin N-acetyltransferase. We utilized a model of a subunit of plant GAPN and the crystallographic structure of human 14-3-3ζ to shape the complex between theses two proteins. Initial dockings were performed with the BiGGER program, which allows an exhaustive search of translational and rotational space. A filtering procedure was then applied to reduce the number of complexes to a manageable number. We predict the structural characteristics of GAPN-14-3-3ζ binding process, proposing that the main attractive force in this complex derives from electrostatic interactions. The predicted model was corroborated by analysis of kinetic behavior of GAPN and its relationship with pH and ionic strength conditions. This study provides a variant on the interaction of 14-3-3 with target proteins, thus affording a wider scenario to establish possible structural models for this remarkable family of regulatory proteins.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science Inc
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
14-3-3 PROTEINS
dc.subject
GAPN
dc.subject
GLYCERALDEHYDE-3-PHOSPHATE
dc.subject
NON-PHOSPHORYLATING
dc.subject
PROTEIN-PROTEIN DOCKING
dc.subject.classification
Bioquímica y Biología Molecular
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
A model for the interaction between plant GAPN and 14-3-3ζ using protein-protein docking calculations, electrostatic potentials and kinetics
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-10-10T19:33:24Z
dc.journal.volume
23
dc.journal.number
6
dc.journal.pagination
490-502
dc.journal.pais
Estados Unidos
dc.description.fil
Fil: Bustos, Diego Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina
dc.description.fil
Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina
dc.journal.title
Journal Of Molecular Graphics & Modelling
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.jmgm.2005.03.002
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1093326305000227
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