Beyond peptides, various classes of lipids are presented for T cell surveillance via the CD1 family. Similarly to T cell receptor (TCR) recognition of peptide-MHC, the broad strokes of antigen-presentation and recognition are similar between the pMHC and lipid-CD1 complexes, whereby the antigen is presented at the apex of the antigen-presenting molecule allowing the exposed loops of the TCR to recognise these upward facing features end-to- end. Significant structural biology research have defined the various methods of lipid antigen presentation to TCRs by the CD1 family, characterising mechanisms of display by cellular and bacterial lipid antigens by each CD1, with a number of crystal structures defining TCR recognition by either direct lipid-CD1 co-recognition or lipid independent models of docking. The antigen binding pocket of CD1c is unique amongst the CD1 family, due to its flexible and porous pocket architecture, with only limited published structural data on lipid display by CD1c available compared to other CD1 molecules. Our team's unpublished structural data of CD1c presentation of cellular gangliosides reveal an atypical mode of presentation, whereby the antigen is presented laterally via a previously uncharacterised sideways portal, away from the typical TCR recognition site. This mode of presentation is observable upon simultaneous presentation of TB lipid mykoketides, which are typically presented upwards. Further, using TCR-trap technology to generate CD1c-TCR complexes for analysis by mass spectrometry have revealed a number of long chain phospholipids, as well as additional bulky headgroup gangliosides, as candidate sideways presenting lipids, which have also been validated structurally. These new modes of lipid presentation may have significant implications in our current dogma of TCR recognition, whereby αβ or γδ TCRs may recognise these sideways presented lipids via a previously uncharacterised mechanism of recognition, or may play a role in non-TCR antigen recognition.