A model for the interaction between plant GAPN and 14-3-3ζ using protein-protein docking calculations, electrostatic potentials and kinetics

Autores
Bustos, Diego Martin; Iglesias, Alberto Alvaro
Año de publicación
2005
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
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
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
Materia
14-3-3 PROTEINS
GAPN
GLYCERALDEHYDE-3-PHOSPHATE
NON-PHOSPHORYLATING
PROTEIN-PROTEIN DOCKING
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/93017
Acceder
id CONICETDig_2c2dc7694257f5bbc5aa2d23a4bac77a
oai_identifier_str oai:ri.conicet.gov.ar:11336/93017
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling A model for the interaction between plant GAPN and 14-3-3ζ using protein-protein docking calculations, electrostatic potentials and kineticsBustos, Diego MartinIglesias, Alberto Alvaro14-3-3 PROTEINSGAPNGLYCERALDEHYDE-3-PHOSPHATENON-PHOSPHORYLATINGPROTEIN-PROTEIN DOCKINGhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Phosphorylated 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.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); ArgentinaFil: 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; ArgentinaElsevier Science Inc2005-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/93017Bustos, 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; 490-5021093-3263CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.jmgm.2005.03.002info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1093326305000227info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:20:26Zoai:ri.conicet.gov.ar:11336/93017instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-15 14:20:27.136CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A model for the interaction between plant GAPN and 14-3-3ζ using protein-protein docking calculations, electrostatic potentials and kinetics
title A model for the interaction between plant GAPN and 14-3-3ζ using protein-protein docking calculations, electrostatic potentials and kinetics
spellingShingle A model for the interaction between plant GAPN and 14-3-3ζ using protein-protein docking calculations, electrostatic potentials and kinetics
Bustos, Diego Martin
14-3-3 PROTEINS
GAPN
GLYCERALDEHYDE-3-PHOSPHATE
NON-PHOSPHORYLATING
PROTEIN-PROTEIN DOCKING
title_short A model for the interaction between plant GAPN and 14-3-3ζ using protein-protein docking calculations, electrostatic potentials and kinetics
title_full A model for the interaction between plant GAPN and 14-3-3ζ using protein-protein docking calculations, electrostatic potentials and kinetics
title_fullStr A model for the interaction between plant GAPN and 14-3-3ζ using protein-protein docking calculations, electrostatic potentials and kinetics
title_full_unstemmed A model for the interaction between plant GAPN and 14-3-3ζ using protein-protein docking calculations, electrostatic potentials and kinetics
title_sort A model for the interaction between plant GAPN and 14-3-3ζ using protein-protein docking calculations, electrostatic potentials and kinetics
dc.creator.none.fl_str_mv Bustos, Diego Martin
Iglesias, Alberto Alvaro
author Bustos, Diego Martin
author_facet Bustos, Diego Martin
Iglesias, Alberto Alvaro
author_role author
author2 Iglesias, Alberto Alvaro
author2_role author
dc.subject.none.fl_str_mv 14-3-3 PROTEINS
GAPN
GLYCERALDEHYDE-3-PHOSPHATE
NON-PHOSPHORYLATING
PROTEIN-PROTEIN DOCKING
topic 14-3-3 PROTEINS
GAPN
GLYCERALDEHYDE-3-PHOSPHATE
NON-PHOSPHORYLATING
PROTEIN-PROTEIN DOCKING
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv 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.
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
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
description 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.
publishDate 2005
dc.date.none.fl_str_mv 2005-06
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/93017
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
1093-3263
CONICET Digital
CONICET
url http://hdl.handle.net/11336/93017
identifier_str_mv 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
1093-3263
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jmgm.2005.03.002
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1093326305000227
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science Inc
publisher.none.fl_str_mv Elsevier Science Inc
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.22299

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