2XN9

Crystal structure of the ternary complex between human T cell receptor, staphylococcal enterotoxin H and human major histocompatibility complex class II

Summary for 2XN9

• Entry DOI: 10.2210/pdb2xn9/pdb
• Related: 1A6A 1AQD 1BX2 1D5M 1D5X 1D5Z 1D6E 1DLH 1ENF 1EWC 1F77 1FV1 1FYT 1H15 1HQR 1HXY 1J8H 1JWM 1JWS 1JWU 1KG0 1KGC 1KLG 1KLU 1KTK 1LO5 1MI5 1OGA 1PYW 1QRN 1R5I 1SEB 1SJE 1SJH 1T5W 1T5X 1YMM 1ZGL 2AK4 2AXH 2BNQ 2BNR 2BNU 2CDE 2CDF 2CDG 2ESV 2EYR 2EYS 2EYT 2G9H 2GJ6 2SEB 2WBJ 2XNA
• Descriptor: T CELL RECEPTOR ALPHA CHAIN C REGION, T CELL RECEPTOR BETA-1 CHAIN C REGION, ENTEROTOXIN H, ... (9 entities in total)
• Functional Keywords: immune system, superantigen, immunoreceptors, ternary complex
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Membrane; Single-pass membrane protein (Potential): P01848 2XN9; Secreted: P01850; Cell membrane; Single-pass type I membrane protein: P0A0M0 P01903
• Total number of polymer chains: 6
• Total formula weight: 120414.59

Authors

Saline, M.,Rodstrom, K.E.J.,Fischer, G.,Orekhov, V.Y.,Karlsson, B.G.,Lindkvist-Petersson, K. (deposition date: 2010-07-31, release date: 2010-11-24, Last modification date: 2024-10-16)

Primary citation

Saline, M.,Rodstrom, K.E.J.,Fischer, G.,Orekhov, V.Y.,Karlsson, B.G.,Lindkvist-Petersson, K.
The Structure of Superantigen Complexed with Tcr and Mhc Reveals Novel Insights Into Superantigenic T Cell Activation.
Nat.Commun., 1:119-, 2010

PubMed Abstract: Superantigens (SAgs) are bacterial toxins that interact with immunoreceptors, T cell receptor (TCR) and major histocompatibility complex (MHC) class II, conventionally through the variable β-domain of TCR (TCRVβ). 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 α-domain of TCR (TCRVα), 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 TCRVα are conserved among other bacterial SAgs. Consequently, a new dimension of SAg biology emerges, suggesting that in addition to the conventional interactions with the TCRVβ domain, SAgs can also activate T cells through the TCRVα domain.

PubMed: 21081917
DOI: 10.1038/NCOMMS1117

Experimental method

X-RAY DIFFRACTION (2.3 Å)