Structure of HLA-A*1101 in complex with a hepatitis B peptide homologue.

Acta Crystallogr Sect F Struct Biol Cryst Commun

Biostructural Research, Department of Medicinal Chemistry, The Danish University of Pharmaceutical Sciences, Universitetsparken 2, DK-2100 Copenhagen, Denmark.

Published: December 2006

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).

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2225367PMC
http://dx.doi.org/10.1107/S1744309106044228DOI Listing

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