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).

• Authors: Thomas Blicher, Jette Sandholm Kastrup, Lars Østergaard Pedersen, Søren Buus, Michael Gajhede
• Journal: Acta crystallographica. Section F, Structural biology and crystallization communications (Acta Crystallogr Sect F Struct Biol Cryst Commun) Vol. 62 Issue Pt 12 Pg. 1179-84 (Dec 01 2006) ISSN: 1744-3091 [Electronic] England
• PMID: 17142892 (Publication Type: Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't)

Chemical References

• HLA-A Antigens
• HLA-A*11:01 antigen
• HLA-A11 Antigen
• Oligopeptides
• Peptide Fragments
• alanyl-isoleucyl-methionyl-prolyl-alanyl-arginyl-phenylalanyl-tyrosyl-prolyl-lysine
• DNA-Directed DNA Polymerase

Topics

• Amino Acid Sequence
• Crystallization
• DNA-Directed DNA Polymerase (chemistry)
• HLA-A Antigens (chemistry)
• HLA-A11 Antigen
• Hepatitis B virus (chemistry)
• Humans
• Hydrogen Bonding
• Oligopeptides (chemistry)
• Peptide Fragments (chemistry)
• Protein Binding
• Protein Conformation