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1seb

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|PDB= 1seb |SIZE=350|CAPTION= <scene name='initialview01'>1seb</scene>, resolution 2.7&Aring;
|PDB= 1seb |SIZE=350|CAPTION= <scene name='initialview01'>1seb</scene>, resolution 2.7&Aring;
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|LIGAND= <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1seb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1seb OCA], [http://www.ebi.ac.uk/pdbsum/1seb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1seb RCSB]</span>
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[[Category: toxin]]
[[Category: toxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:03:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:40:52 2008''

Revision as of 20:40, 30 March 2008


PDB ID 1seb

Drag the structure with the mouse to rotate
, resolution 2.7Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



COMPLEX OF THE HUMAN MHC CLASS II GLYCOPROTEIN HLA-DR1 AND THE BACTERIAL SUPERANTIGEN SEB


Overview

The structure of a bacterial superantigen, Staphylococcus aureus enterotoxin B, bound to a human class II histocompatibility complex molecule (HLA-DR1) has been determined by X-ray crystallography. The superantigen binds as an intact protein outside the conventional peptide antigen-binding site of the class II major histocompatibility complex (MHC) molecule. No large conformational changes occur upon complex formation in either the DR1 or the enterotoxin B molecules. The structure of the complex helps explain how different class II molecules and superantigens associate and suggests a model for ternary complex formation with the T-cell antigen receptor (TCR), in which unconventional TCR-MHC contacts are possible.

About this Structure

1SEB is a Protein complex structure of sequences from Homo sapiens and Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of a human class II histocompatibility molecule complexed with superantigen., Jardetzky TS, Brown JH, Gorga JC, Stern LJ, Urban RG, Chi YI, Stauffacher C, Strominger JL, Wiley DC, Nature. 1994 Apr 21;368(6473):711-8. PMID:8152483

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