2nts
Crystal Structure of SEK-hVb5.1Crystal Structure of SEK-hVb5.1
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSuperantigens (SAGs) interact with host immune receptors to induce a massive release of inflammatory cytokines that can lead to toxic shock syndrome and death. Bacterial SAGs can be classified into five distinct evolutionary groups. Group V SAGs are characterized by the alpha3-beta8 loop, a unique approximately 15 amino acid residue extension that is required for optimal T cell activation. Here, we report the X-ray crystal structures of the group V SAG staphylococcal enterotoxin K (SEK) alone and in complex with the TCR hVbeta5.1 domain. SEK adopts a unique TCR binding orientation relative to other SAG-TCR complexes, which results in the alpha3-beta8 loop contacting the apical loop of framework region 4, thereby extending the known TCR recognition site of SAGs. These interactions are absolutely required for TCR binding and T cell activation by SEK, and dictate the TCR Vbeta domain specificity of SEK and other group V SAGs. A novel loop domain in superantigens extends their T cell receptor recognition site.,Gunther S, Varma AK, Moza B, Kasper KJ, Wyatt AW, Zhu P, Rahman AK, Li Y, Mariuzza RA, McCormick JK, Sundberg EJ J Mol Biol. 2007 Aug 3;371(1):210-21. Epub 2007 May 18. PMID:17560605[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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