1an8: Difference between revisions

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==Overview==

Bacterial superantigens are small proteins that have a very potent, stimulatory effect on T lymphocytes through their ability to bind to both, MHC class II molecules and T-cell receptors. We have determined the, three-dimensional structure of a Streptococcal superantigen, SPE-C, at 2.4, A resolution. The structure shows that SPE-C has the usual superantigen, fold, but that the surface that forms a generic, low-affinity MHC-binding, site in other superantigens is here used to create a SPE-C dimer. Instead, MHC class II binding occurs through a zinc binding site that is analogous, to a similar site in staphylococcal enterotoxin A. Consideration of the, SPE-C dimer suggests a novel mechanism for promotion of MHC aggregation, and T-cell activation.

Bacterial superantigens are small proteins that have a very potent stimulatory effect on T lymphocytes through their ability to bind to both MHC class II molecules and T-cell receptors. We have determined the three-dimensional structure of a Streptococcal superantigen, SPE-C, at 2.4 A resolution. The structure shows that SPE-C has the usual superantigen fold, but that the surface that forms a generic, low-affinity MHC-binding site in other superantigens is here used to create a SPE-C dimer. Instead, MHC class II binding occurs through a zinc binding site that is analogous to a similar site in staphylococcal enterotoxin A. Consideration of the SPE-C dimer suggests a novel mechanism for promotion of MHC aggregation and T-cell activation.

==About this Structure==

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[[Category: Single protein]]

[[Category: Streptococcus pyogenes]]

[[Category: Baker, E.N.]]

[[Category: Baker, E N.]]

[[Category: Roussel, A.]]

[[Category: bacterial superantigen]]

[[Category: toxin]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Bacterial superantigens are small proteins that have a very potent, stimulatory effect on T lymphocytes through their ability to bind to both, MHC class II molecules and T-cell receptors. We have determined the, three-dimensional structure of a Streptococcal superantigen, SPE-C, at 2.4, A resolution. The structure shows that SPE-C has the usual superantigen, fold, but that the surface that forms a generic, low-affinity MHC-binding, site in other superantigens is here used to create a SPE-C dimer. Instead, MHC class II binding occurs through a zinc binding site that is analogous, to a similar site in staphylococcal enterotoxin A. Consideration of the, SPE-C dimer suggests a novel mechanism for promotion of MHC aggregation, and T-cell activation.
+Bacterial superantigens are small proteins that have a very potent stimulatory effect on T lymphocytes through their ability to bind to both MHC class II molecules and T-cell receptors. We have determined the three-dimensional structure of a Streptococcal superantigen, SPE-C, at 2.4 A resolution. The structure shows that SPE-C has the usual superantigen fold, but that the surface that forms a generic, low-affinity MHC-binding site in other superantigens is here used to create a SPE-C dimer. Instead, MHC class II binding occurs through a zinc binding site that is analogous to a similar site in staphylococcal enterotoxin A. Consideration of the SPE-C dimer suggests a novel mechanism for promotion of MHC aggregation and T-cell activation.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Single protein]]
 [[Category: Streptococcus pyogenes]]
-[[Category: Baker, E.N.]]
+[[Category: Baker, E N.]]
 [[Category: Roussel, A.]]
 [[Category: bacterial superantigen]]
 [[Category: toxin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:31:03 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:46:18 2008''