1lo5: Difference between revisions
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1esf|1esf]], [[1dlh|1dlh]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lo5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lo5 OCA], [http://www.ebi.ac.uk/pdbsum/1lo5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lo5 RCSB]</span> | |||
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[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
''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 22:05:13 2008'' | ||
Revision as of 22:05, 30 March 2008
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| , resolution 3.20Å | |||||||
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| Related: | 1esf, 1dlh
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the D227A variant of Staphylococcal enterotoxin A in complex with human MHC class II
OverviewOverview
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.
About this StructureAbout this Structure
1LO5 is a Protein complex structure of sequences from Homo sapiens and Staphylococcus aureus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of a SEA variant in complex with MHC class II reveals the ability of SEA to crosslink MHC molecules., Petersson K, Thunnissen M, Forsberg G, Walse B, Structure. 2002 Dec;10(12):1619-26. PMID:12467569
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