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1sbb

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(New page: 200px<br /><applet load="1sbb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sbb, resolution 2.4&Aring;" /> '''T-CELL RECEPTOR BETA ...)
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[[Image:1sbb.gif|left|200px]]<br /><applet load="1sbb" size="350" color="white" frame="true" align="right" spinBox="true"
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'''T-CELL RECEPTOR BETA CHAIN COMPLEXED WITH SUPERANTIGEN SEB'''<br />
'''T-CELL RECEPTOR BETA CHAIN COMPLEXED WITH SUPERANTIGEN SEB'''<br />
==Overview==
==Overview==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SBB OCA].
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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.]]
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[[Category: Mariuzza, R.A.]]
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[[Category: Mariuzza, R A.]]
[[Category: complex]]
[[Category: complex]]
[[Category: superantigen]]
[[Category: superantigen]]
[[Category: t cell receptor]]
[[Category: t cell receptor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:14:37 2007''
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''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


1sbb, resolution 2.4Å

Drag the structure with the mouse to rotate

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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