Crystal structure of a superantigen bound to MHC class II displays zinc and peptide dependence
(2001) In EMBO Journal 20(13). p.3306-3312- Abstract
The three-dimensional structure of a bacterial superantigen, Staphylococcus aureus enterotoxin H (SEH), bound to human major histocompatibility complex (MHC) class II (HLA-DR1) has been determined by X-ray crystallography to 2.6 Å resolution (1HXY). The superantigen binds on top of HLA-DR1 in a completely different way from earlier co-crystallized superantigens from S. aureus. SEH interacts with high affinity through a zinc ion with the β1 chain of HLA-DR1 and also with the peptide presented by HLA-DR1. The structure suggests that all superantigens interacting with MHC class II in a zinc-dependent manner present the superantigen in a common way. This suggests a new model for ternary complex formation with the T-cell receptor (TCR), in... (More)
The three-dimensional structure of a bacterial superantigen, Staphylococcus aureus enterotoxin H (SEH), bound to human major histocompatibility complex (MHC) class II (HLA-DR1) has been determined by X-ray crystallography to 2.6 Å resolution (1HXY). The superantigen binds on top of HLA-DR1 in a completely different way from earlier co-crystallized superantigens from S. aureus. SEH interacts with high affinity through a zinc ion with the β1 chain of HLA-DR1 and also with the peptide presented by HLA-DR1. The structure suggests that all superantigens interacting with MHC class II in a zinc-dependent manner present the superantigen in a common way. This suggests a new model for ternary complex formation with the T-cell receptor (TCR), in which a contact between the TCR and the MHC class II is unlikely.
(Less)
- author
- Petersson, Karin LU ; Håkansson, Maria LU ; Nilsson, Helen LU ; Forsberg, Göran ; Svensson, L Anders ; Liljas, Anders LU and Walse, Björn LU
- organization
- publishing date
- 2001-07-02
- type
- Contribution to journal
- publication status
- published
- keywords
- MHC class II, Staphylococcal enterotoxin, Superantigen, X-ray crystallography, Zinc
- in
- EMBO Journal
- volume
- 20
- issue
- 13
- pages
- 7 pages
- publisher
- Oxford University Press
- external identifiers
-
- scopus:0035796399
- pmid:11432818
- ISSN
- 0261-4189
- DOI
- 10.1093/emboj/20.13.3306
- language
- English
- LU publication?
- yes
- id
- 89122858-f622-41dc-a3a2-2ddec3dca351
- date added to LUP
- 2017-02-15 15:41:59
- date last changed
- 2024-02-12 13:02:19
@article{89122858-f622-41dc-a3a2-2ddec3dca351,
abstract = {{<p>The three-dimensional structure of a bacterial superantigen, Staphylococcus aureus enterotoxin H (SEH), bound to human major histocompatibility complex (MHC) class II (HLA-DR1) has been determined by X-ray crystallography to 2.6 Å resolution (1HXY). The superantigen binds on top of HLA-DR1 in a completely different way from earlier co-crystallized superantigens from S. aureus. SEH interacts with high affinity through a zinc ion with the β1 chain of HLA-DR1 and also with the peptide presented by HLA-DR1. The structure suggests that all superantigens interacting with MHC class II in a zinc-dependent manner present the superantigen in a common way. This suggests a new model for ternary complex formation with the T-cell receptor (TCR), in which a contact between the TCR and the MHC class II is unlikely.</p>}},
author = {{Petersson, Karin and Håkansson, Maria and Nilsson, Helen and Forsberg, Göran and Svensson, L Anders and Liljas, Anders and Walse, Björn}},
issn = {{0261-4189}},
keywords = {{MHC class II; Staphylococcal enterotoxin; Superantigen; X-ray crystallography; Zinc}},
language = {{eng}},
month = {{07}},
number = {{13}},
pages = {{3306--3312}},
publisher = {{Oxford University Press}},
series = {{EMBO Journal}},
title = {{Crystal structure of a superantigen bound to MHC class II displays zinc and peptide dependence}},
url = {{http://dx.doi.org/10.1093/emboj/20.13.3306}},
doi = {{10.1093/emboj/20.13.3306}},
volume = {{20}},
year = {{2001}},
}