Figure 1
Comparison of the HA1.7 TCR CDR loop conformations pre and post ligation to DR1 and DR4.
(A) Superposition of the unligated HA1.7 TCR (green) with the ligated conformations of the HA1.7 TCR when bound to DR1 (yellow) and DR4 (blue). (B) Conformation of the HA1.7 TCR CDR loops comparing ligated and unligated structures (colors as in (A)). (C&D) A view of the superimposed CDR loops from the perspective of the TCR contacting a stick representation of the HA306–318 peptide (red). Green loops are the unligated HA1.7 CDR loops, yellow are HA1.7 CDR loops when ligated to DR1 (C) and blue are HA1.7 CDR loops when ligated to DR4 (D). (E&F) HA1.7 CDR1β contacting the HA306–318 residue, 315K, presented by either DR1 (E) or DR4 (F). Green loops are the unligated HA1.7 CDR loops, yellow are HA1.7 CDR loops when ligated to DR1 and blue are HA1.7 CDR loops when ligated to DR4. Contact distances were smaller, allowing salt bridge formation, between the TCR and 315K in the TCR ligated forms.
