2xna | pdb_00002xna

Crystal structure of the complex between human T cell receptor and staphylococcal enterotoxin

spinqualitylabelsall models 2xna, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2xna is a 3 chain structure with sequence from "micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885 and Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, NA Related: 1enf, 2esv, 1f77, 1qrn, 1kgc, 2bnr, 2ak4, 2gj6, 2cdg, 2bnu, 2eys, 1mi5, 2cdf, 1fyt, 1ymm, 1ewc, 1j8h, 1zgl, 2axh, 1ktk, 2eyt, 2bnq, 1oga, 2eyr, 2cde, 2xn9 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ETXH_STAAU] Staphylococcal enterotoxins cause the intoxication staphylococcal food poisoning syndrome. The illness characterized by high fever, hypotension, diarrhea, shock, and in some cases death. Publication Abstract from PubMed Superantigens (SAgs) are bacterial toxins that interact with immunoreceptors, T cell receptor (TCR) and major histocompatibility complex (MHC) class II, conventionally through the variable beta-domain of TCR (TCRVbeta). They induce a massive release of cytokines, which can lead to diseases such as food poisoning and toxic shock syndrome. In this study, we report the X-ray structure of the ternary complex between staphylococcal enterotoxin H (SEH) and its human receptors, MHC class II and TCR. The structure demonstrates that SEH predominantly interacts with the variable alpha-domain of TCR (TCRValpha), which is supported by nuclear magnetic resonance (NMR) analyses. Furthermore, there is no contact between MHC and TCR upon complex formation. Structural analyses suggest that the major contact points to TCRValpha are conserved among other bacterial SAgs. Consequently, a new dimension of SAg biology emerges, suggesting that in addition to the conventional interactions with the TCRVbeta domain, SAgs can also activate T cells through the TCRValpha domain. The structure of superantigen complexed with TCR and MHC reveals novel insights into superantigenic T cell activation.,Saline M, Rodstrom KE, Fischer G, Orekhov VY, Karlsson BG, Lindkvist-Petersson K Nat Commun. 2010 Nov 16;1:119. PMID:21081917 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also T-cell receptor T-cell receptor 3D structures

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