Fig. 3.

Structural comparison of 1F1E8hu and JM22 TcRs. (a) Ribbon representation of the 1F1E8hu and JM22 structures colored according to the B-factor, where dark blue is the lowest (15 Å²) and deep red is the highest (75 Å²). (b) Amino acid sequence for the human TcR α-chain constant domain. β-Strands are represented by arrows. The red broken line indicates the disordered region in 1F1E8hu. Residues 159–181 are rainbow colored, reflecting equivalent residues in the C^α domains of JM22 (c) and 1F1E8hu (d). (e) Overlay of the C^α domains of 1F1E8hu (dark gray) and JM22 (light gray), and electron density at 1σ illustrating the shortened DE loop in 1F1E8. Cartoons were produced using PyMOL.