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179 a.a.
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188 a.a.
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13 a.a.
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233 a.a.
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* Residue conservation analysis
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PDB id:
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Immune system/toxin
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Title:
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Crystal structure of the d227a variant of staphylococcal enterotoxin a in complex with human mhc class ii
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Structure:
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Hla class ii histocompatibility antigen, dr alpha chain. Chain: a. Fragment: extracellular domain. Synonym: mhc class ii (hla-dr1, dra 0101)-chain a. Engineered: yes. Hla class ii histocompatibility antigen, dr-1 beta chain. Chain: b. Fragment: extracellular domain. Synonym: mhc class ii (hla-dr1, drb1 0101)-chain b.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: this sequence is peptide from influenza virus, hemagglutinin peptide. Staphylococcus aureus.
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Biol. unit:
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Tetramer (from
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Resolution:
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3.20Å
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R-factor:
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0.245
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R-free:
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0.339
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Authors:
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K.Petersson,M.Thunnissen,G.Forsberg,B.Walse
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Key ref:
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K.Petersson
et al.
(2002).
Crystal structure of a SEA variant in complex with MHC class II reveals the ability of SEA to crosslink MHC molecules.
Structure,
10,
1619-1626.
PubMed id:
DOI:
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Date:
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06-May-02
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Release date:
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18-Dec-02
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PROCHECK
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Headers
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References
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P01903
(DRA_HUMAN) -
HLA class II histocompatibility antigen, DR alpha chain from Homo sapiens
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Seq: Struc:
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254 a.a.
179 a.a.
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P01911
(2B1F_HUMAN) -
HLA class II histocompatibility antigen, DRB1 beta chain from Homo sapiens
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Seq: Struc:
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266 a.a.
188 a.a.*
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DOI no:
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Structure
10:1619-1626
(2002)
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PubMed id:
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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.
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K.Petersson,
M.Thunnissen,
G.Forsberg,
B.Walse.
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ABSTRACT
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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.
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Selected figure(s)
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Figure 3.
Figure 3. Ribbon Representations of the Interfaces between
(A) HLA-DR1, in Green, and SEA[D227A], in Yellow, and (B)
HLA-DR1, in Green, and SEB, in Cyan, as Well as Electrostatic
Interaction and Hydrogen Bond Pattern of Selected Residues in
the Interface 
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2002,
10,
1619-1626)
copyright 2002.
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Figure was
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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D.L.Hu,
K.Omoe,
H.Sashinami,
K.Shinagawa,
and
A.Nakane
(2009).
Immunization with a Nontoxic Mutant of Staphylococcal Enterotoxin A, SEAD227A, Protects against Enterotoxin-Induced Emesis in House Musk Shrews.
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J Infect Dis,
199,
302-310.
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J.Hui,
Y.Cao,
F.Xiao,
J.Zhang,
H.Li,
and
F.Hu
(2008).
Staphylococcus aureus enterotoxin C2 mutants: biological activity assay in vitro.
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J Ind Microbiol Biotechnol,
35,
975-980.
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M.D.Dyer,
T.M.Murali,
and
B.W.Sobral
(2008).
The landscape of human proteins interacting with viruses and other pathogens.
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PLoS Pathog,
4,
e32.
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E.J.Sundberg,
L.Deng,
and
R.A.Mariuzza
(2007).
TCR recognition of peptide/MHC class II complexes and superantigens.
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Semin Immunol,
19,
262-271.
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H.Li,
Y.Zhao,
Y.Guo,
Z.Li,
L.Eisele,
and
W.Mourad
(2007).
Zinc induces dimerization of the class II major histocompatibility complex molecule that leads to cooperative binding to a superantigen.
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J Biol Chem,
282,
5991-6000.
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PDB code:
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S.Günther,
A.K.Varma,
B.Moza,
K.J.Kasper,
A.W.Wyatt,
P.Zhu,
A.K.Rahman,
Y.Li,
R.A.Mariuzza,
J.K.McCormick,
and
E.J.Sundberg
(2007).
A novel loop domain in superantigens extends their T cell receptor recognition site.
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J Mol Biol,
371,
210-221.
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PDB codes:
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D.D.Pless,
G.Ruthel,
E.K.Reinke,
R.G.Ulrich,
and
S.Bavari
(2005).
Persistence of zinc-binding bacterial superantigens at the surface of antigen-presenting cells contributes to the extreme potency of these superantigens as T-cell activators.
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Infect Immun,
73,
5358-5366.
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K.Petersson,
G.Forsberg,
and
B.Walse
(2004).
Interplay between superantigens and immunoreceptors.
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Scand J Immunol,
59,
345-355.
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Y.Zhao,
Z.Li,
S.J.Drozd,
Y.Guo,
W.Mourad,
and
H.Li
(2004).
Crystal structure of Mycoplasma arthritidis mitogen complexed with HLA-DR1 reveals a novel superantigen fold and a dimerized superantigen-MHC complex.
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Structure,
12,
277-288.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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');
}
}
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