1dyq
From Proteopedia
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|PDB= 1dyq |SIZE=350|CAPTION= <scene name='initialview01'>1dyq</scene>, resolution 1.50Å | |PDB= 1dyq |SIZE=350|CAPTION= <scene name='initialview01'>1dyq</scene>, resolution 1.50Å | ||
|SITE= <scene name='pdbsite=ZN1:Zn+Binding+Site+The+Zn+Ion+Is+Bound+To+Residues+HIS+A+18+...'>ZN1</scene> | |SITE= <scene name='pdbsite=ZN1:Zn+Binding+Site+The+Zn+Ion+Is+Bound+To+Residues+HIS+A+18+...'>ZN1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dyq OCA], [http://www.ebi.ac.uk/pdbsum/1dyq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dyq RCSB]</span> | ||
}} | }} | ||
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[[Category: Rupp, B.]] | [[Category: Rupp, B.]] | ||
[[Category: Segelke, B W.]] | [[Category: Segelke, B W.]] | ||
| - | [[Category: SO4]] | ||
| - | [[Category: ZN]] | ||
[[Category: enterotoxin]] | [[Category: enterotoxin]] | ||
[[Category: staphylococcal enterotoxin type some]] | [[Category: staphylococcal enterotoxin type some]] | ||
[[Category: vaccine]] | [[Category: vaccine]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:51:41 2008'' |
Revision as of 16:51, 30 March 2008
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| , resolution 1.50Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STAPHYLOCOCCAL ENTEROTOXIN A MUTANT VACCINE
Overview
Staphylococcal enterotoxins (SEs) are superantigenic protein toxins responsible for a number of life-threatening diseases. The X-ray structure of a staphylococcal enterotoxin A (SEA) triple-mutant (L48R, D70R, and Y92A) vaccine reveals a cascade of structural rearrangements located in three loop regions essential for binding the alpha subunit of major histocompatibility complex class II (MHC-II) molecules. A comparison of hypothetical model complexes between SEA and the SEA triple mutant with MHC-II HLA-DR1 clearly shows disruption of key ionic and hydrophobic interactions necessary for forming the complex. Extensive dislocation of the disulfide loop in particular interferes with MHC-IIalpha binding. The triple-mutant structure provides new insights into the loss of superantigenicity and toxicity of an engineered superantigen and provides a basis for further design of enterotoxin vaccines.
About this Structure
1DYQ is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
Structural basis for abrogated binding between staphylococcal enterotoxin A superantigen vaccine and MHC-IIalpha., Krupka HI, Segelke BW, Ulrich RG, Ringhofer S, Knapp M, Rupp B, Protein Sci. 2002 Mar;11(3):642-51. PMID:11847286
Page seeded by OCA on Sun Mar 30 19:51:41 2008
