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. Author manuscript; available in PMC: 2013 Nov 1.
Published in final edited form as: Immunol Rev. 2012 Nov;250(1):102–119. doi: 10.1111/j.1600-065X.2012.01161.x

Fig. 2. TCRαβ dockings onto pMHCI molecules.

Fig. 2

(A, B) Side and top views, respectively, of three TCR/pMHCII complexes (adapted from 29). For clarity, only one MHCI peptide-binding groove is shown. The N15 TCR is in white (PDB 1NFD), the 2C TCR in red (PDB 2CKB), and the A6 TCR in green (PDB 1QSE). Relative to the MHC molecule, the three TCR molecules have a similar diagonal docking with Vα and Vβ domains on α2 and α1 helices, respectively. The orientation difference can be described by parameters of twist, tilt, and shift. (C) The TCR docking constraint imposed by the MHC molecule is shown by the two arrows indicating the high points on α1 and α2 helices. The helical breaks are caused by the inherent left-handed twist of the β sheet seen at the bottom of peptide-binding groove.