Exchange catalysis by tapasin exploits conserved and allele-specific features of MHC-I molecules

Tapasin is part of the peptide loading complex necessary for presenting antigenic peptides on MHC-I for the induction of adaptive immunity. Here the authors show that tapasin interacts with MHC-I in both conserved and allele-specific regions to promote antigen presentation, with tapasin L18 and K16...

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Autores principales: Huan Lan, Esam T. Abualrous, Jana Sticht, Laura Maria Arroyo Fernandez, Tamina Werk, Christoph Weise, Martin Ballaschk, Peter Schmieder, Bernhard Loll, Christian Freund
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Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/8bd32bbbde944e95a968d72ae29445ed
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spelling oai:doaj.org-article:8bd32bbbde944e95a968d72ae29445ed2021-12-02T16:14:57ZExchange catalysis by tapasin exploits conserved and allele-specific features of MHC-I molecules10.1038/s41467-021-24401-42041-1723https://doaj.org/article/8bd32bbbde944e95a968d72ae29445ed2021-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-24401-4https://doaj.org/toc/2041-1723Tapasin is part of the peptide loading complex necessary for presenting antigenic peptides on MHC-I for the induction of adaptive immunity. Here the authors show that tapasin interacts with MHC-I in both conserved and allele-specific regions to promote antigen presentation, with tapasin L18 and K16 residues both implicated in this molecular interaction.Huan LanEsam T. AbualrousJana StichtLaura Maria Arroyo FernandezTamina WerkChristoph WeiseMartin BallaschkPeter SchmiederBernhard LollChristian FreundNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Huan Lan
Esam T. Abualrous
Jana Sticht
Laura Maria Arroyo Fernandez
Tamina Werk
Christoph Weise
Martin Ballaschk
Peter Schmieder
Bernhard Loll
Christian Freund
Exchange catalysis by tapasin exploits conserved and allele-specific features of MHC-I molecules
description Tapasin is part of the peptide loading complex necessary for presenting antigenic peptides on MHC-I for the induction of adaptive immunity. Here the authors show that tapasin interacts with MHC-I in both conserved and allele-specific regions to promote antigen presentation, with tapasin L18 and K16 residues both implicated in this molecular interaction.
format article
author Huan Lan
Esam T. Abualrous
Jana Sticht
Laura Maria Arroyo Fernandez
Tamina Werk
Christoph Weise
Martin Ballaschk
Peter Schmieder
Bernhard Loll
Christian Freund
author_facet Huan Lan
Esam T. Abualrous
Jana Sticht
Laura Maria Arroyo Fernandez
Tamina Werk
Christoph Weise
Martin Ballaschk
Peter Schmieder
Bernhard Loll
Christian Freund
author_sort Huan Lan
title Exchange catalysis by tapasin exploits conserved and allele-specific features of MHC-I molecules
title_short Exchange catalysis by tapasin exploits conserved and allele-specific features of MHC-I molecules
title_full Exchange catalysis by tapasin exploits conserved and allele-specific features of MHC-I molecules
title_fullStr Exchange catalysis by tapasin exploits conserved and allele-specific features of MHC-I molecules
title_full_unstemmed Exchange catalysis by tapasin exploits conserved and allele-specific features of MHC-I molecules
title_sort exchange catalysis by tapasin exploits conserved and allele-specific features of mhc-i molecules
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/8bd32bbbde944e95a968d72ae29445ed
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