Functioning as a key component of antigen presentation, the major histocompatibility complex (MHC) is crucial for the elicitation of immune responses. Understanding the biology and interactions of these molecules is key in understanding immunity as a whole. Although not as well understood as their classical counterparts, non-classical MHC molecules have only been recently shown to be immunologically relevant due to their tissue restriction and highly specialised functions. Our group has recently characterised H2-Q10, a murine non-classical MHC molecule, which shows overexpression in the liver. Of particular interest is a novel interaction that occurs between H2-Q10 and the CD8aa homodimer expressed on gamma delta T cells. We have shown that this interaction is dependent on the glycosylation signature of CD8aa, with N-glycosylation implicated as the key pathway controlling recognition. We have also observed that the a3 domain of H2-Q10 is the point of contact for CD8aa binding and further determined key residues within the a3 domain that regulate this interaction. Our results have provided insight into the biochemical signature governing the novel interaction between H2-Q10 and CD8aa and opens up further studies data into elucidating the immunological consequences of this interaction on gamma delta T cells and immunity.