Open AccessStructure of HLA‐A*1101 in complex with a hepatitis B peptide homologue
Author(s) -
Blicher Thomas,
Kastrup Jette Sandholm,
Pedersen Lars Østergaard,
Buus Søren,
Gajhede Michael
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106044228
Subject(s) - peptide , peptide sequence , human leukocyte antigen , sequence (biology) , virology , chemistry , dna , biology , binding site , microbiology and biotechnology , biochemistry , gene , genetics , antigen
A high‐resolution structure of the human MHC‐I molecule HLA‐A*1101 is presented in which it forms a complex with a sequence homologue of a peptide that occurs naturally in hepatitis B virus DNA polymerase. The sequence of the bound peptide is AIMPARFYPK, while that of the corresponding natural peptide is LIMPARFYPK. The peptide does not make efficient use of the middle E pocket for binding, which leads to a rather superficial and exposed binding mode for the central peptide residues. Despite this, the peptide binds with high affinity (IC 50 of 31 n M ).