1sbb: Difference between revisions
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sbb OCA], [http://www.ebi.ac.uk/pdbsum/1sbb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sbb RCSB]</span> | |||
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[[Category: t cell receptor]] | [[Category: t cell receptor]] | ||
''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 23:39:44 2008'' | ||
Revision as of 23:39, 30 March 2008
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| , resolution 2.4Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
T-CELL RECEPTOR BETA CHAIN COMPLEXED WITH SUPERANTIGEN SEB
OverviewOverview
Superantigens (SAGs) are a class of immunostimulatory proteins of bacterial or viral origin that activate T cells by binding to the V beta domain of the T cell antigen receptor (TCR). The three-dimensional structure of the complex between a TCR beta chain (mouse V beta8.2) and the SAG staphylococcal enterotoxin B (SEB) at 2.4 A resolution reveals why SEB recognizes only certain V beta families, as well as why only certain SAGs bind mouse V beta8.2. Models of the TCR-SEB-peptide/MHC class II complex indicate that V alpha interacts with the MHC beta chain in the TCR-SAG-MHC complex. The extent of the interaction is variable and is largely determined by the geometry of V alpha/V beta domain association. This variability can account for the preferential expression of certain V alpha regions among T cells reactive with SEB.
About this StructureAbout this Structure
1SBB is a Protein complex structure of sequences from Mus musculus and Staphylococcus aureus. Full crystallographic information is available from OCA.
ReferenceReference
Three-dimensional structure of the complex between a T cell receptor beta chain and the superantigen staphylococcal enterotoxin B., Li H, Llera A, Tsuchiya D, Leder L, Ysern X, Schlievert PM, Karjalainen K, Mariuzza RA, Immunity. 1998 Dec;9(6):807-16. PMID:9881971
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