Structural analysis of the TPI-Manchester, a thermolabile variant of human triosephosphate isomerase

Autores
Romero, Jorge Miguel
Año de publicación
2024
Idioma
español castellano
Tipo de recurso
artículo
Estado
versión publicada
Descripción
This is a preprint article, it offers immediate access but has not been peer reviewed. All content on this site: Copyright © 2023 Elsevier Inc., its licensors, and contributors. All rights are reserved, including those for text and data mining, AI training, and similar technologies. For all open access content, the Creative Commons licensing terms apply.
Fil: Romero, Jorge Miguel. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica Ranwel Caputto, Argentina.
Fil: Romero, Jorge Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones en Química Biológica de Córdoba, Argentina.
Human triosephosphate isomerase G122R, also known as TPI-Manchester, is a thermolabile variant detected in a screening of more than 3,400 individuals from a population in Ann Arbor, Michigan. Here, the crystallographic structure of G122R was solved to determine the molecular basis of its thermal stability. Structural analysis revealed an increase in the flexibility of residues at the dimer interface, even though R122 is about 20 Å away, suggesting that long-range electrostatic interactions may play a key role in the mutation effect.
info:eu-repo/semantics/publishedVersion
Fil: Romero, Jorge Miguel. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica Ranwel Caputto, Argentina.
Fil: Romero, Jorge Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones en Química Biológica de Córdoba, Argentina.
Materia
Triosephosphate isomerase deficiency
X-ray crystallization
Stability
Flexibility
Nivel de accesibilidad
acceso abierto
Condiciones de uso
Repositorio
Repositorio Digital Universitario (UNC)
Institución
Universidad Nacional de Córdoba
OAI Identificador
oai:rdu.unc.edu.ar:11086/552351
Acceder
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oai_identifier_str oai:rdu.unc.edu.ar:11086/552351
network_acronym_str RDUUNC
repository_id_str 2572
network_name_str Repositorio Digital Universitario (UNC)
spelling Structural analysis of the TPI-Manchester, a thermolabile variant of human triosephosphate isomeraseRomero, Jorge MiguelTriosephosphate isomerase deficiencyX-ray crystallizationStabilityFlexibilityThis is a preprint article, it offers immediate access but has not been peer reviewed. All content on this site: Copyright © 2023 Elsevier Inc., its licensors, and contributors. All rights are reserved, including those for text and data mining, AI training, and similar technologies. For all open access content, the Creative Commons licensing terms apply.Fil: Romero, Jorge Miguel. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica Ranwel Caputto, Argentina.Fil: Romero, Jorge Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones en Química Biológica de Córdoba, Argentina.Human triosephosphate isomerase G122R, also known as TPI-Manchester, is a thermolabile variant detected in a screening of more than 3,400 individuals from a population in Ann Arbor, Michigan. Here, the crystallographic structure of G122R was solved to determine the molecular basis of its thermal stability. Structural analysis revealed an increase in the flexibility of residues at the dimer interface, even though R122 is about 20 Å away, suggesting that long-range electrostatic interactions may play a key role in the mutation effect.info:eu-repo/semantics/publishedVersionFil: Romero, Jorge Miguel. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica Ranwel Caputto, Argentina.Fil: Romero, Jorge Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones en Química Biológica de Córdoba, Argentina.SSRN - Elsevier2024-05-30info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfRomero, Jorge Miguel, Structural Analysis of the Tpi-Manchester, a Thermolabile Variant of Human Triosephosphate Isomerase. Available at SSRN: https://ssrn.com/abstract=4848610 or http://dx.doi.org/10.2139/ssrn.4848610http://hdl.handle.net/11086/552351https://papers.ssrn.com/sol3/papers.cfm?abstract_id=4848610http://dx.doi.org/10.2139/ssrn.4848610spainfo:eu-repo/semantics/openAccessreponame:Repositorio Digital Universitario (UNC)instname:Universidad Nacional de Córdobainstacron:UNC2025-09-29T13:42:24Zoai:rdu.unc.edu.ar:11086/552351Institucionalhttps://rdu.unc.edu.ar/Universidad públicaNo correspondehttp://rdu.unc.edu.ar/oai/snrdoca.unc@gmail.comArgentinaNo correspondeNo correspondeNo correspondeopendoar:25722025-09-29 13:42:24.969Repositorio Digital Universitario (UNC) - Universidad Nacional de Córdobafalse
dc.title.none.fl_str_mv Structural analysis of the TPI-Manchester, a thermolabile variant of human triosephosphate isomerase
title Structural analysis of the TPI-Manchester, a thermolabile variant of human triosephosphate isomerase
spellingShingle Structural analysis of the TPI-Manchester, a thermolabile variant of human triosephosphate isomerase
Romero, Jorge Miguel
Triosephosphate isomerase deficiency
X-ray crystallization
Stability
Flexibility
title_short Structural analysis of the TPI-Manchester, a thermolabile variant of human triosephosphate isomerase
title_full Structural analysis of the TPI-Manchester, a thermolabile variant of human triosephosphate isomerase
title_fullStr Structural analysis of the TPI-Manchester, a thermolabile variant of human triosephosphate isomerase
title_full_unstemmed Structural analysis of the TPI-Manchester, a thermolabile variant of human triosephosphate isomerase
title_sort Structural analysis of the TPI-Manchester, a thermolabile variant of human triosephosphate isomerase
dc.creator.none.fl_str_mv Romero, Jorge Miguel
author Romero, Jorge Miguel
author_facet Romero, Jorge Miguel
author_role author
dc.subject.none.fl_str_mv Triosephosphate isomerase deficiency
X-ray crystallization
Stability
Flexibility
topic Triosephosphate isomerase deficiency
X-ray crystallization
Stability
Flexibility
dc.description.none.fl_txt_mv This is a preprint article, it offers immediate access but has not been peer reviewed. All content on this site: Copyright © 2023 Elsevier Inc., its licensors, and contributors. All rights are reserved, including those for text and data mining, AI training, and similar technologies. For all open access content, the Creative Commons licensing terms apply.
Fil: Romero, Jorge Miguel. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica Ranwel Caputto, Argentina.
Fil: Romero, Jorge Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones en Química Biológica de Córdoba, Argentina.
Human triosephosphate isomerase G122R, also known as TPI-Manchester, is a thermolabile variant detected in a screening of more than 3,400 individuals from a population in Ann Arbor, Michigan. Here, the crystallographic structure of G122R was solved to determine the molecular basis of its thermal stability. Structural analysis revealed an increase in the flexibility of residues at the dimer interface, even though R122 is about 20 Å away, suggesting that long-range electrostatic interactions may play a key role in the mutation effect.
info:eu-repo/semantics/publishedVersion
Fil: Romero, Jorge Miguel. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica Ranwel Caputto, Argentina.
Fil: Romero, Jorge Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones en Química Biológica de Córdoba, Argentina.
description This is a preprint article, it offers immediate access but has not been peer reviewed. All content on this site: Copyright © 2023 Elsevier Inc., its licensors, and contributors. All rights are reserved, including those for text and data mining, AI training, and similar technologies. For all open access content, the Creative Commons licensing terms apply.
publishDate 2024
dc.date.none.fl_str_mv 2024-05-30
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
status_str publishedVersion
format article
dc.identifier.none.fl_str_mv Romero, Jorge Miguel, Structural Analysis of the Tpi-Manchester, a Thermolabile Variant of Human Triosephosphate Isomerase. Available at SSRN: https://ssrn.com/abstract=4848610 or http://dx.doi.org/10.2139/ssrn.4848610
http://hdl.handle.net/11086/552351
https://papers.ssrn.com/sol3/papers.cfm?abstract_id=4848610
http://dx.doi.org/10.2139/ssrn.4848610
identifier_str_mv Romero, Jorge Miguel, Structural Analysis of the Tpi-Manchester, a Thermolabile Variant of Human Triosephosphate Isomerase. Available at SSRN: https://ssrn.com/abstract=4848610 or http://dx.doi.org/10.2139/ssrn.4848610
url http://hdl.handle.net/11086/552351
https://papers.ssrn.com/sol3/papers.cfm?abstract_id=4848610
http://dx.doi.org/10.2139/ssrn.4848610
dc.language.none.fl_str_mv spa
language spa
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv SSRN - Elsevier
publisher.none.fl_str_mv SSRN - Elsevier
dc.source.none.fl_str_mv reponame:Repositorio Digital Universitario (UNC)
instname:Universidad Nacional de Córdoba
instacron:UNC
reponame_str Repositorio Digital Universitario (UNC)
collection Repositorio Digital Universitario (UNC)
instname_str Universidad Nacional de Córdoba
instacron_str UNC
institution UNC
repository.name.fl_str_mv Repositorio Digital Universitario (UNC) - Universidad Nacional de Córdoba
repository.mail.fl_str_mv oca.unc@gmail.com
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score 13.070432

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