title: The composition of the F pocket in HLA-A*74 generates C-terminal promiscuity among its bound peptides.
abstract: In this study we sequenced the bound peptides from three alleles belonging to the HLA-A*74 group (HLA-A*74:04, A*74:06 and A*74:07) that are distinguished by four polymorphic residues within the peptide-binding region. Our data illustrates that A*74:04 exhibits preference for L, M or I at P2 and L, S or P at PΩ, while for A*74:07 the P2 anchor prefers L, P or I and the PΩ anchor S, P, L. In contrast A*74:06 features a P2 anchor motif of S or L, while a PΩ anchor could not be defined; however, a preference for polar residues S, T, Q or the charged residue R at the PΩ position could be detected.
authors.affiliation: Institute for Transfusion Medicine, Hannover Medical School, Hannover, Germany. bade-doeding.christina@mh-hannover.de
authors.forename: C
authors.initials: C
authors.lastname: Bade-Doeding
authors.forename: T
authors.initials: T
authors.lastname: Huyton
authors.forename: B
authors.initials: B
authors.lastname: Eiz-Vesper
authors.forename: R
authors.initials: R
authors.lastname: Blasczyk
mesh_terms: D000483:Alleles; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D001665:Binding Sites; D015234:HLA-A Antigens / Q000737:chemistry / Q000235:genetics* / Q000276:immunology; D006801:Humans; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000235:genetics* / Q000276:immunology
chemical_list: D015234:HLA-A Antigens; D010455:Peptides