Defining the structural basis for human alloantibody binding to human leukocyte antigen allele HLA-A*11:01
Anti-human leukocyte antigen (HLA) antibodies are important mediators of alloresponses, but structural insights on antibody:HLA interaction are still lacking. Here the authors provide a 2.4 Å structure of antibody:HLA complex, and also analyse HLA features important for other HLA-interacting molecul...
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Nature Portfolio
2019
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oai:doaj.org-article:d43685122a4b496da7e60656bb9c199a2021-12-02T14:40:20ZDefining the structural basis for human alloantibody binding to human leukocyte antigen allele HLA-A*11:0110.1038/s41467-019-08790-12041-1723https://doaj.org/article/d43685122a4b496da7e60656bb9c199a2019-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-08790-1https://doaj.org/toc/2041-1723Anti-human leukocyte antigen (HLA) antibodies are important mediators of alloresponses, but structural insights on antibody:HLA interaction are still lacking. Here the authors provide a 2.4 Å structure of antibody:HLA complex, and also analyse HLA features important for other HLA-interacting molecules, to enhance our understanding of alloimmunity.Yue GuYee Hwa WongChong Wai LiewConrad E. Z. ChanTanusya M. MuraliJiawei YapChien Tei TooKiren PurushotormanMaryam HamidiniaAbbas El SahiliAngeline T. H. GohRachel Z. C. TeoKathryn J. WoodBrendon J. HansonNicholas R. J. GascoigneJulien LescarAnantharaman VathsalaPaul A. MacAryNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-11 (2019) |
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Science Q Yue Gu Yee Hwa Wong Chong Wai Liew Conrad E. Z. Chan Tanusya M. Murali Jiawei Yap Chien Tei Too Kiren Purushotorman Maryam Hamidinia Abbas El Sahili Angeline T. H. Goh Rachel Z. C. Teo Kathryn J. Wood Brendon J. Hanson Nicholas R. J. Gascoigne Julien Lescar Anantharaman Vathsala Paul A. MacAry Defining the structural basis for human alloantibody binding to human leukocyte antigen allele HLA-A*11:01 |
description |
Anti-human leukocyte antigen (HLA) antibodies are important mediators of alloresponses, but structural insights on antibody:HLA interaction are still lacking. Here the authors provide a 2.4 Å structure of antibody:HLA complex, and also analyse HLA features important for other HLA-interacting molecules, to enhance our understanding of alloimmunity. |
format |
article |
author |
Yue Gu Yee Hwa Wong Chong Wai Liew Conrad E. Z. Chan Tanusya M. Murali Jiawei Yap Chien Tei Too Kiren Purushotorman Maryam Hamidinia Abbas El Sahili Angeline T. H. Goh Rachel Z. C. Teo Kathryn J. Wood Brendon J. Hanson Nicholas R. J. Gascoigne Julien Lescar Anantharaman Vathsala Paul A. MacAry |
author_facet |
Yue Gu Yee Hwa Wong Chong Wai Liew Conrad E. Z. Chan Tanusya M. Murali Jiawei Yap Chien Tei Too Kiren Purushotorman Maryam Hamidinia Abbas El Sahili Angeline T. H. Goh Rachel Z. C. Teo Kathryn J. Wood Brendon J. Hanson Nicholas R. J. Gascoigne Julien Lescar Anantharaman Vathsala Paul A. MacAry |
author_sort |
Yue Gu |
title |
Defining the structural basis for human alloantibody binding to human leukocyte antigen allele HLA-A*11:01 |
title_short |
Defining the structural basis for human alloantibody binding to human leukocyte antigen allele HLA-A*11:01 |
title_full |
Defining the structural basis for human alloantibody binding to human leukocyte antigen allele HLA-A*11:01 |
title_fullStr |
Defining the structural basis for human alloantibody binding to human leukocyte antigen allele HLA-A*11:01 |
title_full_unstemmed |
Defining the structural basis for human alloantibody binding to human leukocyte antigen allele HLA-A*11:01 |
title_sort |
defining the structural basis for human alloantibody binding to human leukocyte antigen allele hla-a*11:01 |
publisher |
Nature Portfolio |
publishDate |
2019 |
url |
https://doaj.org/article/d43685122a4b496da7e60656bb9c199a |
work_keys_str_mv |
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