2XNA

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

Summary for 2XNA

• Entry DOI: 10.2210/pdb2xna/pdb
• Related: 1ENF 1EWC 1F77 1FYT 1J8H 1KGC 1KTK 1MI5 1OGA 1QRN 1YMM 1ZGL 2AK4 2AXH 2BNQ 2BNR 2BNU 2CDE 2CDF 2CDG 2ESV 2EYR 2EYS 2EYT 2GJ6 2XN9
• Descriptor: T CELL RECEPTOR ALPHA CHAIN C REGION, T CELL RECEPTOR BETA-1 CHAIN C REGION, ENTEROTOXIN H, ... (6 entities in total)
• Functional Keywords: immune system, superantigen
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Membrane; Single-pass membrane protein (Potential): P01848 2XNA; Secreted: P01850
• Total number of polymer chains: 3
• Total formula weight: 75579.12

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: 2023-12-20)

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 (2.1 Å)