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

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).

SUBMITTER: Blicher T

PROVIDER: S-EPMC2225367 | biostudies-literature | 2006 Dec

REPOSITORIES: biostudies-literature

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

Blicher Thomas T Kastrup Jette Sandholm JS Pedersen Lars Østergaard LØ Buus Søren S Gajhede Michael M

Acta crystallographica. Section F, Structural biology and crystallization communications 20061104 Pt 12

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 thi ...[more]

PMID: 17142892

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