학술논문
The composition of the F pocket in HLA-A*74 generates C-terminal promiscuity among its bound peptides.
Document Type
Article
Author
Source
Subject
*PEPTIDES
*PROTEIN binding
*PROMISCUITY
*HLA histocompatibility antigens
*GENETIC polymorphisms
*NUCLEOTIDE sequence
*AMINO acids
*BIOINFORMATICS
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Language
ISSN
0001-2815
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. [ABSTRACT FROM AUTHOR]