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Crystal structure of a superantigen bound to MHC class II displays zinc and peptide dependence

Petersson, Karin LU ; Håkansson, Maria LU ; Nilsson, Helen LU ; Forsberg, Göran ; Svensson, L Anders ; Liljas, Anders LU and Walse, Björn LU (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.

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author
; ; ; ; ; and
organization
publishing date
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
  • pmid:11432818
  • scopus:0035796399
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
2022-03-16 20:12:25
@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}},
}