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).
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Crystallization
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DNA-Directed DNA Polymerase / chemistry*
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HLA-A Antigens / chemistry*
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HLA-A11 Antigen
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Hepatitis B virus / chemistry
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Humans
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Hydrogen Bonding
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Oligopeptides / chemistry*
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Peptide Fragments / chemistry*
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Protein Binding
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Protein Conformation
Substances
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HLA-A Antigens
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HLA-A*11:01 antigen
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HLA-A11 Antigen
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Oligopeptides
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Peptide Fragments
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alanyl-isoleucyl-methionyl-prolyl-alanyl-arginyl-phenylalanyl-tyrosyl-prolyl-lysine
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DNA-Directed DNA Polymerase