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PDBsum entry 1lo5
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Immune system/toxin
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PDB id
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1lo5
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Contents |
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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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References listed in PDB file
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Key reference
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Title
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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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Authors
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K.Petersson,
M.Thunnissen,
G.Forsberg,
B.Walse.
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Ref.
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Structure, 2002,
10,
1619-1626.
[DOI no: ]
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PubMed id
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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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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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