Pathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding

Human leucocyte antigen E (HLA-E) directly engages NK cells but also presents antigen to CD8+ T cells. Here the authors show crystal structures of HLA-E in complex with peptides derived from HIV and Mycobacterium tuberculosis, and describe binding conformations, the positional impact of residues inv...

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Autores principales: Lucy C. Walters, Karl Harlos, Simon Brackenridge, Daniel Rozbesky, Jordan R. Barrett, Vitul Jain, Thomas S. Walter, Chris A. O’Callaghan, Persephone Borrow, Mireille Toebes, Scott G. Hansen, Jonah B Sacha, Shaheed Abdulhaqq, Justin M. Greene, Klaus Früh, Emily Marshall, Louis J. Picker, E. Yvonne Jones, Andrew J. McMichael, Geraldine M. Gillespie
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Publicado: Nature Portfolio 2018
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Acceso en línea:https://doaj.org/article/c538b7f0bce048839998f3c2c728defd
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spelling oai:doaj.org-article:c538b7f0bce048839998f3c2c728defd2021-12-02T16:49:31ZPathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding10.1038/s41467-018-05459-z2041-1723https://doaj.org/article/c538b7f0bce048839998f3c2c728defd2018-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-05459-zhttps://doaj.org/toc/2041-1723Human leucocyte antigen E (HLA-E) directly engages NK cells but also presents antigen to CD8+ T cells. Here the authors show crystal structures of HLA-E in complex with peptides derived from HIV and Mycobacterium tuberculosis, and describe binding conformations, the positional impact of residues involved and discuss implications for functional presentation to CD8+ T cells.Lucy C. WaltersKarl HarlosSimon BrackenridgeDaniel RozbeskyJordan R. BarrettVitul JainThomas S. WalterChris A. O’CallaghanPersephone BorrowMireille ToebesScott G. HansenJonah B SachaShaheed AbdulhaqqJustin M. GreeneKlaus FrühEmily MarshallLouis J. PickerE. Yvonne JonesAndrew J. McMichaelGeraldine M. GillespieNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Lucy C. Walters
Karl Harlos
Simon Brackenridge
Daniel Rozbesky
Jordan R. Barrett
Vitul Jain
Thomas S. Walter
Chris A. O’Callaghan
Persephone Borrow
Mireille Toebes
Scott G. Hansen
Jonah B Sacha
Shaheed Abdulhaqq
Justin M. Greene
Klaus Früh
Emily Marshall
Louis J. Picker
E. Yvonne Jones
Andrew J. McMichael
Geraldine M. Gillespie
Pathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding
description Human leucocyte antigen E (HLA-E) directly engages NK cells but also presents antigen to CD8+ T cells. Here the authors show crystal structures of HLA-E in complex with peptides derived from HIV and Mycobacterium tuberculosis, and describe binding conformations, the positional impact of residues involved and discuss implications for functional presentation to CD8+ T cells.
format article
author Lucy C. Walters
Karl Harlos
Simon Brackenridge
Daniel Rozbesky
Jordan R. Barrett
Vitul Jain
Thomas S. Walter
Chris A. O’Callaghan
Persephone Borrow
Mireille Toebes
Scott G. Hansen
Jonah B Sacha
Shaheed Abdulhaqq
Justin M. Greene
Klaus Früh
Emily Marshall
Louis J. Picker
E. Yvonne Jones
Andrew J. McMichael
Geraldine M. Gillespie
author_facet Lucy C. Walters
Karl Harlos
Simon Brackenridge
Daniel Rozbesky
Jordan R. Barrett
Vitul Jain
Thomas S. Walter
Chris A. O’Callaghan
Persephone Borrow
Mireille Toebes
Scott G. Hansen
Jonah B Sacha
Shaheed Abdulhaqq
Justin M. Greene
Klaus Früh
Emily Marshall
Louis J. Picker
E. Yvonne Jones
Andrew J. McMichael
Geraldine M. Gillespie
author_sort Lucy C. Walters
title Pathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding
title_short Pathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding
title_full Pathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding
title_fullStr Pathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding
title_full_unstemmed Pathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding
title_sort pathogen-derived hla-e bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding
publisher Nature Portfolio
publishDate 2018
url https://doaj.org/article/c538b7f0bce048839998f3c2c728defd
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