L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction

L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction

L-Amino acid Transporters (LATs) are asymmetric amino acid exchangers. Here the authors determine the crystal structure of a prokaryotic LAT, the alanine-serine-cysteine exchanger (BasC) and identify key residues for asymmetric substrate interaction in both BasC and the homologous human transporter...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Ekaitz Errasti-Murugarren, Joana Fort, Paola Bartoccioni, Lucía Díaz, Els Pardon, Xavier Carpena, Meritxell Espino-Guarch, Antonio Zorzano, Christine Ziegler, Jan Steyaert, Juan Fernández-Recio, Ignacio Fita, Manuel Palacín
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2019
Materias:
Science
Q
Acceso en línea:https://doaj.org/article/02f00387781745f491d1d369e1db2215
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:02f00387781745f491d1d369e1db2215
record_format dspace
spelling oai:doaj.org-article:02f00387781745f491d1d369e1db22152021-12-02T16:58:13ZL amino acid transporter structure and molecular bases for the asymmetry of substrate interaction10.1038/s41467-019-09837-z2041-1723https://doaj.org/article/02f00387781745f491d1d369e1db22152019-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-09837-zhttps://doaj.org/toc/2041-1723L-Amino acid Transporters (LATs) are asymmetric amino acid exchangers. Here the authors determine the crystal structure of a prokaryotic LAT, the alanine-serine-cysteine exchanger (BasC) and identify key residues for asymmetric substrate interaction in both BasC and the homologous human transporter Asc-1 through functional studies.Ekaitz Errasti-MurugarrenJoana FortPaola BartoccioniLucía DíazEls PardonXavier CarpenaMeritxell Espino-GuarchAntonio ZorzanoChristine ZieglerJan SteyaertJuan Fernández-RecioIgnacio FitaManuel PalacínNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Ekaitz Errasti-Murugarren
Joana Fort
Paola Bartoccioni
Lucía Díaz
Els Pardon
Xavier Carpena
Meritxell Espino-Guarch
Antonio Zorzano
Christine Ziegler
Jan Steyaert
Juan Fernández-Recio
Ignacio Fita
Manuel Palacín
L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction
description L-Amino acid Transporters (LATs) are asymmetric amino acid exchangers. Here the authors determine the crystal structure of a prokaryotic LAT, the alanine-serine-cysteine exchanger (BasC) and identify key residues for asymmetric substrate interaction in both BasC and the homologous human transporter Asc-1 through functional studies.
format article
author Ekaitz Errasti-Murugarren
Joana Fort
Paola Bartoccioni
Lucía Díaz
Els Pardon
Xavier Carpena
Meritxell Espino-Guarch
Antonio Zorzano
Christine Ziegler
Jan Steyaert
Juan Fernández-Recio
Ignacio Fita
Manuel Palacín
author_facet Ekaitz Errasti-Murugarren
Joana Fort
Paola Bartoccioni
Lucía Díaz
Els Pardon
Xavier Carpena
Meritxell Espino-Guarch
Antonio Zorzano
Christine Ziegler
Jan Steyaert
Juan Fernández-Recio
Ignacio Fita
Manuel Palacín
author_sort Ekaitz Errasti-Murugarren
title L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction
title_short L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction
title_full L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction
title_fullStr L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction
title_full_unstemmed L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction
title_sort l amino acid transporter structure and molecular bases for the asymmetry of substrate interaction
publisher Nature Portfolio
publishDate 2019
url https://doaj.org/article/02f00387781745f491d1d369e1db2215
work_keys_str_mv AT ekaitzerrastimurugarren laminoacidtransporterstructureandmolecularbasesfortheasymmetryofsubstrateinteraction
AT joanafort laminoacidtransporterstructureandmolecularbasesfortheasymmetryofsubstrateinteraction
AT paolabartoccioni laminoacidtransporterstructureandmolecularbasesfortheasymmetryofsubstrateinteraction
AT luciadiaz laminoacidtransporterstructureandmolecularbasesfortheasymmetryofsubstrateinteraction
AT elspardon laminoacidtransporterstructureandmolecularbasesfortheasymmetryofsubstrateinteraction
AT xaviercarpena laminoacidtransporterstructureandmolecularbasesfortheasymmetryofsubstrateinteraction
AT meritxellespinoguarch laminoacidtransporterstructureandmolecularbasesfortheasymmetryofsubstrateinteraction
AT antoniozorzano laminoacidtransporterstructureandmolecularbasesfortheasymmetryofsubstrateinteraction
AT christineziegler laminoacidtransporterstructureandmolecularbasesfortheasymmetryofsubstrateinteraction
AT jansteyaert laminoacidtransporterstructureandmolecularbasesfortheasymmetryofsubstrateinteraction
AT juanfernandezrecio laminoacidtransporterstructureandmolecularbasesfortheasymmetryofsubstrateinteraction
AT ignaciofita laminoacidtransporterstructureandmolecularbasesfortheasymmetryofsubstrateinteraction
AT manuelpalacin laminoacidtransporterstructureandmolecularbasesfortheasymmetryofsubstrateinteraction
_version_ 1718382367782993920

Ejemplares similares