Abstract:
:Staphylococcal enterotoxins and toxic shock syndrome toxin-1 are known as superantigens due to their ability to activate a large number of T-cells by crosslinking the major histocompatibility complex class II molecules with the T-cell receptor. Although superantigens seem to act by a common mechanism, they vary in many of their specific interactions and biological properties. A structural comparison of staphylococcal enterotoxins A and C2, members of the staphylococcal superantigens, has shown large conformational differences at the putative TcR interaction site (loops between alphaN-alpha2, alpha4-beta9 and beta10-alpha5 in staphylococcal enterotoxin A) that could explain the variability in their T-cell receptor specificity. A common Zn2(+)-binding site was identified in both staphylococcal enterotoxin A and C2 that is superimposable but differs somewhat in its coordination geometry between the two molecules.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Schad EM,Papageorgiou AC,Svensson LA,Acharya KRdoi
10.1006/jmbi.1997.1023subject
Has Abstractpub_date
1997-06-06 00:00:00pages
270-80issue
2eissn
0022-2836issn
1089-8638pii
S0022-2836(97)91023-8journal_volume
269pub_type
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