2ntt

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2ntt, resolution 1.561Å

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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 with and as ligands. 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 May 18;. PMID:17560605

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