1sbb
From Proteopedia
(New page: 200px<br /><applet load="1sbb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sbb, resolution 2.4Å" /> '''T-CELL RECEPTOR BETA ...) |
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| - | [[Image:1sbb.gif|left|200px]]<br /><applet load="1sbb" size=" | + | [[Image:1sbb.gif|left|200px]]<br /><applet load="1sbb" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1sbb, resolution 2.4Å" /> | caption="1sbb, resolution 2.4Å" /> | ||
'''T-CELL RECEPTOR BETA CHAIN COMPLEXED WITH SUPERANTIGEN SEB'''<br /> | '''T-CELL RECEPTOR BETA CHAIN COMPLEXED WITH SUPERANTIGEN SEB'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Superantigens (SAGs) are a class of immunostimulatory proteins of | + | 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 Structure== | ==About this Structure== | ||
| - | 1SBB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http:// | + | 1SBB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SBB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
[[Category: Li, H.]] | [[Category: Li, H.]] | ||
| - | [[Category: Mariuzza, R | + | [[Category: Mariuzza, R A.]] |
[[Category: complex]] | [[Category: complex]] | ||
[[Category: superantigen]] | [[Category: superantigen]] | ||
[[Category: t cell receptor]] | [[Category: t cell receptor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:59:42 2008'' |
Revision as of 12:59, 21 February 2008
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T-CELL RECEPTOR BETA CHAIN COMPLEXED WITH SUPERANTIGEN SEB
Overview
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 Structure
1SBB is a Protein complex structure of sequences from Mus musculus and Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
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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