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HLA Class I residues that contact the antigenic peptide and/or the TCR
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Residue #DomainPocketPeptide bindingTCR contact
51AX -
71A, B X-
91B, C X-
241B X-
251B X-
341B X-
451B X-
581- -X
591A X-
631A, BX-
651--X
661A, B XX
671BX-
681--X
691-XX
701A, B, CX-
721--X
731CX-
741CX-
761-X-
771FX-
801FX-
811FX-
841FX-
972C, E X-
992A, B, DX-
1142D, E X-
1162FX-
1232FX-
1332E--
1432FX-
1462FX-
1472E, F X-
1492--X
1502-XX
1512--X
1522EX-
1552-XX
1562D, E X-
1582--X
1592A, D XX
1602DX-
1622---
1632AXX
1662--X
1672AXX
1702--X
1712AX-

Legend

Table 1 shows the assignment of residues to the α1 or α2 domains, to the peptide binding site, specificity pockets, and to the contact region for the TCR. In the column "Peptide" those residues are indicated, which are solvent-accessible, and which thus potentially have contact with bound peptides. It corresponds to Table 14 of the study published Saper et al. In the column "Pocket" the assignment of residues to the respective pockets is given according to Saper et al. Although that study contained no assignment for the residues 69, 76, 150, 155, for HistoCheck these residues were nevertheless weighted as peptide-binding since they are potentially involved in peptide binding due to their solvent accessibility.

Position 133 is located at the bottom of pocket E, and is conserved in HLA-A, B and C (January 2003). Although having been assigned to pocket E by Saper et al., this residue is not solvent-accessible and thus has no contact with bound peptides. Accordingly, for HistoCheck this position was not weighted as peptide-binding despite its assignment to pocket E.

The assignment to the contact region for the TCR is based on the study published by Garboczi et al.
In addition it must be noted that a residue may be assigned to several pockets, and at the same time also the contact region for the TCR.

Table 2 >>>