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leukocyte antigen (HLA)-C*06:02 is identified as the allele associated with the highest risk for the development of the autoimmune skin disease psoriasis. However, the diversity and mode of peptide presentation by the HLA-C*06:02 molecule remains unclear. Here, we describe the endogenous peptide repertoire of \u223c3,000 sequences for HLA-C*06:02 that defines the peptide-binding motif for this HLA allomorph. We found that HLA-C*06:02 predominantly presents nonamer peptides with dominant arginine anchors at the P2 and P7 positions and a preference for small hydrophobic residues at the C terminus (P\u03a9). To determine the structural basis of this selectivity, we determined crystal structures of HLA-C*06:02 in complex with two self-peptides (ARTELYRSL and ARFNDLRFV) and an analogue of a melanocyte autoantigen (ADAMTSL5, VRSRR-abu-LRL) implicated in psoriasis. These structures revealed that HLA-C*06:02 possesses a deep peptide-binding groove comprising two electronegative B- and E-pockets that coincide with the preference for P2 and P7 arginine anchors. The ADAMTSL5 autoantigen possessed a P7-Leu instead of the P7-Arg residue, but nevertheless was accommodated within the HLA-C*06:02 antigen-binding cleft. Collectively, our results provide the structural basis for understanding peptide repertoire selection in HLA-C*06:02.","bibjson":{"author":[{"initials":"JI","lastname":"Mobbs","name":"Mobbs JI"},{"initials":"PT","lastname":"Illing","name":"Illing PT"},{"initials":"NL","lastname":"Dudek","name":"Dudek NL"},{"initials":"AG","lastname":"Brooks","name":"Brooks AG"},{"initials":"DG","lastname":"Baker","name":"Baker DG"},{"initials":"AW","lastname":"Purcell","name":"Purcell AW"},{"initials":"J","lastname":"Rossjohn","name":"Rossjohn J"},{"initials":"JP","lastname":"Vivian","name":"Vivian JP"}],"identifier":[{"id":"10.1074/jbc.M117.806976","type":"doi"},{"id":"28855257","type":"pubmed"}],"issue":[null],"journal":{"iso_abbreviation":"J. Biol. 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