Figure 5: Spatial configuration of MHC class I-presented C14nef5 and conventional peptides.
From: Crystal structure of the N-myristoylated lipopeptide-bound MHC class I complex
(a) A stereo view of C14nef5 (thick yellow sticks) bound to Mamu-B*098 overlaid with an array of representative 9-mer peptides (thin lines) bound to MHC class I molecules is shown. (b) The space coordinates of the main chain of MHC class I-bound peptides were determined for 280 registered MHC class I:peptide complexes and the mean values on the x axis (parallel to two α-helixes), y axis (vertical to the x axis and parallel to the line connecting the centres of two α-helixes) and z axis (vertical to the x axis and y axis) are shown with open circles. Error bars indicate s.d. The space coordinates of Mamu-B*098-bound C14nef5 were also determined and are shown with closed circles. It is worth noting that the three C-terminal residues (Ala3, Ile4 and Ser5) of C14nef5 and corresponding amino acid residues of conventional peptides exhibited a similar spatial configuration, whereas the two N-terminal residues (Gly1 and Gly2) of C14nef5 deviated in the y- and z axes from the position of the corresponding residues of conventional peptides.
