2NTT
Crystal Structure of SEK
Summary for 2NTT
| Entry DOI | 10.2210/pdb2ntt/pdb |
| Related | 2NTS |
| Descriptor | Staphylococcal enterotoxin K, CHLORIDE ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | superantigen; t cell receptor, toxin |
| Biological source | Staphylococcus aureus subsp. aureus |
| Total number of polymer chains | 2 |
| Total formula weight | 51241.09 |
| Authors | Gunther, S.,Varma, A.K.,Moza, B.,Sundberg, E.J. (deposition date: 2006-11-08, release date: 2007-06-26, Last modification date: 2024-04-03) |
| Primary citation | Gunther, S.,Varma, A.K.,Moza, B.,Kasper, K.J.,Wyatt, A.W.,Zhu, P.,Rahman, A.K.,Li, Y.,Mariuzza, R.A.,McCormick, J.K.,Sundberg, E.J. A novel loop domain in superantigens extends their T cell receptor recognition site J.Mol.Biol., 371:210-221, 2007 Cited by PubMed Abstract: 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. PubMed: 17560605DOI: 10.1016/j.jmb.2007.05.038 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.561 Å) |
Structure validation
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