CD8+ T cells play an important role in the immune response to SARS-CoV-2 infection and vaccination. Following the identification of several SARS-CoV-2 derived CD8+ T cell epitopes for several HLA class I alleles, recent studies have revealed surprisingly varied characteristics of associated CD8+ T cell responses. The molecular basis for CD8+ T cell recognition of SARS-CoV-2 derived epitopes which ultimately determines the Repertoire diversity and quality of T cell responses remains unclear. Following SARS-CoV-2 infection or vaccination the SARS-CoV-2 derived S269-277 peptide elicits a dominant CD8+ T cell response in carriers of the common HLA-A2 allele. Since HLA-A2S269-277-specific CD8+ T cells utilise a biased TRAV12 gene usage, we sought to understand the molecular basis for this TRAV12 dominance. We expressed and refolded four TRAV12+ TCRs which bound the HLA-A2S269-277 complex high affinity. We determined the crystal structure of the HLA-A2S269-277 binary complex and subsequently the ternary structure of a TRAV12+ TCR bound to HLA-A2S269-277. The TRAV12+ TCR docked atop HLA-A2 with standard docking polarity, whereupon HLA-A2S269-277 recognition was dominated by both TRAV12 germline-encoded residues and residues from conserved sequence motifs located within the CDR3a and CDR3b loops. Here, the TCR made extensive contacts along the entire length of the S269-277 peptide, suggesting that the TRAV12+TCRs would be sensitive to any sequence variation within this epitope. To examine this, we investigated cross-reactivity towards analogous peptides from existing SARS-CoV-2 variants and closely related coronaviruses. We show, via surface plasmon resonance and tetramer studies, that the TRAV12+ T cell repertoire cross-reacts poorly with these analogous epitopes. Overall, we defined the structural basis underpinning biased TCR recognition of CD8+ T cells directed at an immunodominant HLA-A2S269-277 epitope and provide a framework for understanding TCR cross-reactivity towards viral variants within S269-277 peptide.