Structure of HLA-A*1101 in complex with a hepatitis B peptide homologue.
作者信息
Blicher Thomas, Kastrup Jette Sandholm, Pedersen Lars Østergaard, Buus Søren, Gajhede Michael
机构信息
Biostructural Research, Department of Medicinal Chemistry, The Danish University of Pharmaceutical Sciences, Universitetsparken 2, DK-2100 Copenhagen, Denmark.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Dec 1;62(Pt 12):1179-84. doi: 10.1107/S1744309106044228. Epub 2006 Nov 4.
Abstract
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).
摘要
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