2ntt
From Proteopedia
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[[Image:2ntt.gif|left|200px]] | [[Image:2ntt.gif|left|200px]] | ||
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'''Crystal Structure of SEK''' | '''Crystal Structure of SEK''' | ||
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[[Category: Sundberg, E J.]] | [[Category: Sundberg, E J.]] | ||
[[Category: Varma, A K.]] | [[Category: Varma, A K.]] | ||
| - | [[Category: | + | [[Category: Superantigen]] |
| - | [[Category: | + | [[Category: T cell receptor]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:54:15 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 06:54, 4 May 2008
Crystal Structure of SEK
Overview
Superantigens (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.
About this Structure
2NTT is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sun May 4 09:54:15 2008
