A New Angle on TCR Activation

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A New Angle on TCR Activation Jia-huai Wang, Ellis L. Reinherz Immunity Volume 35, Issue 5, Pages 658-660 (November 2011) DOI: 10.1016/j.immuni.2011.11.008 Copyright © 2011 Elsevier Inc. Terms and Conditions

Figure 1 Superposition of Crystal Structures of 3A1-Ld-42F3 with QL9-Ld-42F3 Shown here are the α1 and α2 domains of MHC molecule Ld in complex with the 42F3 TCR αβ heterodimer. Only 3A1 peptide (SPLDSLWWI) is shown for clarity in the peptide-binding groove. TCR 42F3 heterodimeric subunits in the 3A1-Ld-42F3 complex are in dark green (β subunit) and light green (α subunit), respectively, and in red (β subunit) and purple (α subunit) in the QL9-Ld-42F3 complex. The superposition shown is based on the MHC structure. Immunity 2011 35, 658-660DOI: (10.1016/j.immuni.2011.11.008) Copyright © 2011 Elsevier Inc. Terms and Conditions