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Crystal structure of a SEA variant in complex with MHC class II reveals the ability of SEA to crosslink MHC molecules

Lindkvist, Karin LU ; Thunnissen, Marjolein LU ; Forsberg, G and Walse, B (2002) In Structure 10(12). p.1619-1626
Abstract
Although the biological properties of staphylococcal enterotoxin A (SEA) have been well characterized, structural insights into the interaction between SEA and major histocompatibilty complex (MHC) class II have only been obtained by modeling. Here, the crystal structure of the D227A variant of SEA in complex with human MHC class II has been determined by X-ray crystallography. SEA(D227A) exclusively binds with its N-terminal domain to the alpha chain of HLA-DR1. The ability of one SEA molecule to crosslink two MHC molecules was modeled. It shows that this SEA molecule cannot interact with the T cell receptor (TCR) while a second SEA molecule interacts with MHC. Because of its relatively low toxicity, the D227A variant of SEA is used in... (More)
Although the biological properties of staphylococcal enterotoxin A (SEA) have been well characterized, structural insights into the interaction between SEA and major histocompatibilty complex (MHC) class II have only been obtained by modeling. Here, the crystal structure of the D227A variant of SEA in complex with human MHC class II has been determined by X-ray crystallography. SEA(D227A) exclusively binds with its N-terminal domain to the alpha chain of HLA-DR1. The ability of one SEA molecule to crosslink two MHC molecules was modeled. It shows that this SEA molecule cannot interact with the T cell receptor (TCR) while a second SEA molecule interacts with MHC. Because of its relatively low toxicity, the D227A variant of SEA is used in tumor therapy. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
enterotoxin, staphylococcal, SEA, MHC class II, protein-protein interaction, superantigen, X-ray crystallography
in
Structure
volume
10
issue
12
pages
1619 - 1626
publisher
Cell Press
external identifiers
  • wos:000182039500005
  • pmid:12467569
  • scopus:0036901549
ISSN
0969-2126
DOI
10.1016/S0969-2126(02)00895-X
language
English
LU publication?
yes
id
c65e7e29-59c9-4ceb-b8fa-0b995181b05e (old id 313885)
date added to LUP
2007-11-08 15:47:53
date last changed
2017-03-05 03:28:16
@article{c65e7e29-59c9-4ceb-b8fa-0b995181b05e,
  abstract     = {Although the biological properties of staphylococcal enterotoxin A (SEA) have been well characterized, structural insights into the interaction between SEA and major histocompatibilty complex (MHC) class II have only been obtained by modeling. Here, the crystal structure of the D227A variant of SEA in complex with human MHC class II has been determined by X-ray crystallography. SEA(D227A) exclusively binds with its N-terminal domain to the alpha chain of HLA-DR1. The ability of one SEA molecule to crosslink two MHC molecules was modeled. It shows that this SEA molecule cannot interact with the T cell receptor (TCR) while a second SEA molecule interacts with MHC. Because of its relatively low toxicity, the D227A variant of SEA is used in tumor therapy.},
  author       = {Lindkvist, Karin and Thunnissen, Marjolein and Forsberg, G and Walse, B},
  issn         = {0969-2126},
  keyword      = {enterotoxin,staphylococcal,SEA,MHC class II,protein-protein interaction,superantigen,X-ray crystallography},
  language     = {eng},
  number       = {12},
  pages        = {1619--1626},
  publisher    = {Cell Press},
  series       = {Structure},
  title        = {Crystal structure of a SEA variant in complex with MHC class II reveals the ability of SEA to crosslink MHC molecules},
  url          = {http://dx.doi.org/10.1016/S0969-2126(02)00895-X},
  volume       = {10},
  year         = {2002},
}