1an8: Difference between revisions

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[[Image:1an8.jpg|left|200px]]
{{Seed}}
[[Image:1an8.png|left|200px]]


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{{STRUCTURE_1an8|  PDB=1an8  |  SCENE=  }}  
{{STRUCTURE_1an8|  PDB=1an8  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THE STREPTOCOCCAL SUPERANTIGEN SPE-C'''
===CRYSTAL STRUCTURE OF THE STREPTOCOCCAL SUPERANTIGEN SPE-C===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_9253413}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 9253413 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9253413}}


==About this Structure==
==About this Structure==
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[[Category: Bacterial superantigen]]
[[Category: Bacterial superantigen]]
[[Category: Toxin]]
[[Category: Toxin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:28:25 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:12:26 2008''
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