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

Research output: Contribution to journalJournal articleResearchpeer-review

Thomas Blicher, Jette Sandholm Kastrup, Lars Østergaard Pedersen, Søren Buus, Michael Gajhede

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).
Original languageEnglish
JournalActa Crystallographica Section F-Structural Biology and Crystallization Communications
Volume62
Issue numberPt 12
Pages (from-to)1179-84
Number of pages5
DOIs
Publication statusPublished - 2006

Bibliographical note

Keywords: Amino Acid Sequence; Crystallization; DNA-Directed DNA Polymerase; HLA-A Antigens; Hepatitis B virus; Humans; Hydrogen Bonding; Oligopeptides; Peptide Fragments; Protein Binding; Protein Conformation

ID: 9942600