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1.  Structure of HLA-A*1101 in complex with a hepatitis B peptide homologue 
The structure of HLA-A*1101 in complex with a HBV peptide homologue is presented and discussed in the context of vaccine design.
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 (IC50 of 31 nM).
doi:10.1107/S1744309106044228
PMCID: PMC2225367  PMID: 17142892
HLA-A*1101; major histocompatibility complex class I; hepatitis B; HBV; peptide decamer; vaccine development

Results 1-1 (1)