TY - JOUR
T1 - Structure of HLA-A*1101 in complex with a hepatitis B peptide homologue
AU - Blicher, Thomas
AU - Kastrup, Jette Sandholm
AU - Pedersen, Lars Østergaard
AU - Buus, Søren
AU - Gajhede, Michael
N1 - 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
PY - 2006
Y1 - 2006
N2 - 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).
AB - 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).
U2 - 10.1107/S1744309106044228
DO - 10.1107/S1744309106044228
M3 - Journal article
C2 - 17142892
SN - 2053-230X
VL - 62
SP - 1179
EP - 1184
JO - Acta Crystallographica Section F: Structural Biology Communications
JF - Acta Crystallographica Section F: Structural Biology Communications
IS - Pt 12
ER -
