In naïve mice, the TCR repertoire for the immunodominant influenza epitope, nucleoprotein (NP₃₆₆), contains a high proportion of TRBV17+ TCRs. By contrast after influenza infection, the repertoire exhibits recruitment and expansion of TRBV13+ but avoidance of TRBV17+ TCRs. Previously, we defined structures for two TRBV17+ TCRs from the naïve repertoire in complex with H-2D^b-NP₃₆₆ and these TCRs bound in a completely reversed orientation to canonical TCR:peptide-MHC docking topology. This suggests reverse-docking is associated with poor recruitment into the immune response during influenza infection but it is not known whether structural constraints imposed by TCR docking onto peptide-MHC are causative of poor recruitment. We propose that the reverse-docking topology negatively affects formation of the immunological synapse by reducing TCR affinity and/or abrogating efficient binding of the CD8 co-receptor. Here, we assess the molecular and structural requirements for effective recruitment of CD8 T cells during influenza infection using TCR retrogenic mice to express various TCRs with distinct features; including docking orientation, affinity to H-2D^b-NP₃₆₆ and dependence on the CD8 co-receptor. We thereby aim to define the structural and molecular features that are required for efficient recruitment of CD8 T cells during the immune response to influenza.