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...
| Main Authors: | , , , , , , , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2018-08-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-018-05459-z |
| _version_ | 1818994752522027008 |
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| 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 |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-20T21:02:57Z |
| format | Article |
| id | doaj.art-c538b7f0bce048839998f3c2c728defd |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-20T21:02:57Z |
| publishDate | 2018-08-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-c538b7f0bce048839998f3c2c728defd2022-12-21T19:26:40ZengNature PortfolioNature Communications2041-17232018-08-019111310.1038/s41467-018-05459-zPathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide bindingLucy C. Walters0Karl Harlos1Simon Brackenridge2Daniel Rozbesky3Jordan R. Barrett4Vitul Jain5Thomas S. Walter6Chris A. O’Callaghan7Persephone Borrow8Mireille Toebes9Scott G. Hansen10Jonah B Sacha11Shaheed Abdulhaqq12Justin M. Greene13Klaus Früh14Emily Marshall15Louis J. Picker16E. Yvonne Jones17Andrew J. McMichael18Geraldine M. Gillespie19Nuffield Department of Medicine Research Building, Roosevelt Drive, Nuffield Department of Medicine, University of OxfordDivision of Structural Biology, Wellcome Centre for Human Genetics, Roosevelt Drive, University of OxfordNuffield Department of Medicine Research Building, Roosevelt Drive, Nuffield Department of Medicine, University of OxfordDivision of Structural Biology, Wellcome Centre for Human Genetics, Roosevelt Drive, University of OxfordNuffield Department of Medicine Research Building, Roosevelt Drive, Nuffield Department of Medicine, University of OxfordDivision of Structural Biology, Wellcome Centre for Human Genetics, Roosevelt Drive, University of OxfordDivision of Structural Biology, Wellcome Centre for Human Genetics, Roosevelt Drive, University of OxfordHenry Wellcome Building for Molecular Physiology, University of OxfordNuffield Department of Medicine Research Building, Roosevelt Drive, Nuffield Department of Medicine, University of OxfordDepartment Molecular Oncology and Immunology, B6 Plesmanlaan 121Vaccine and Gene Therapy Institute and Oregon National Primate Research Center, Oregon Health & Science UniversityVaccine and Gene Therapy Institute and Oregon National Primate Research Center, Oregon Health & Science UniversityVaccine and Gene Therapy Institute and Oregon National Primate Research Center, Oregon Health & Science UniversityVaccine and Gene Therapy Institute and Oregon National Primate Research Center, Oregon Health & Science UniversityVaccine and Gene Therapy Institute and Oregon National Primate Research Center, Oregon Health & Science UniversityVaccine and Gene Therapy Institute and Oregon National Primate Research Center, Oregon Health & Science UniversityVaccine and Gene Therapy Institute and Oregon National Primate Research Center, Oregon Health & Science UniversityDivision of Structural Biology, Wellcome Centre for Human Genetics, Roosevelt Drive, University of OxfordNuffield Department of Medicine Research Building, Roosevelt Drive, Nuffield Department of Medicine, University of OxfordNuffield Department of Medicine Research Building, Roosevelt Drive, Nuffield Department of Medicine, University of OxfordHuman 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.https://doi.org/10.1038/s41467-018-05459-z |
| spellingShingle | 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 Nature Communications |
| title | 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_short | 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 |
| url | https://doi.org/10.1038/s41467-018-05459-z |
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