Fig. 7: Conformational changes in TCRs and pMHC after complex formation. | Nature Communications

Fig. 7: Conformational changes in TCRs and pMHC after complex formation.

From: Structural assessment of HLA-A2-restricted SARS-CoV-2 spike epitopes recognized by public and private T-cell receptors

Fig. 7

a Structural rearrangements in CDR3β and CDR3α of RLQ3 (unbound pRLQ3, yellow; bound RLQ3, light green or pink) induced by binding to RLQ–HLA-A2 (RLQ, orange; HLA-A2, gray). Hydrogen bonds are red dotted lines. Double-headed red arrow indicates region of structural shifts. b Structural rearrangements in CDR1α and CDR2α of RLQ3. c Superposition of the Cα domain of TCR YLQ7 in unbound form and in complex with YLQ–HLA-A2 (unbound YLQ7, yellow; bound YLQ7, blue). Double-headed red arrow indicates site of structural differences in Cα associated with YLQ–HLA-A2 binding. d Superposition of YLQ–HLA-A2 in unbound form and in complex with TCR YLQ7 showing rearrangements in residues P4–P7 of the YLQ peptide induced by YLQ7 binding (unbound YLQ, gray or violet; bound YLQ, cyan; HLA-A2, gray).

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