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

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Standard

Structure of HLA-A*1101 in complex with a hepatitis B peptide homologue. / Blicher, Thomas; Kastrup, Jette Sandholm; Pedersen, Lars Østergaard; Buus, Søren; Gajhede, Michael.

In: Acta Crystallographica Section F-Structural Biology and Crystallization Communications, Vol. 62, No. Pt 12, 2006, p. 1179-84.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Blicher, T, Kastrup, JS, Pedersen, LØ, Buus, S & Gajhede, M 2006, 'Structure of HLA-A*1101 in complex with a hepatitis B peptide homologue', Acta Crystallographica Section F-Structural Biology and Crystallization Communications, vol. 62, no. Pt 12, pp. 1179-84. https://doi.org/10.1107/S1744309106044228

APA

Blicher, T., Kastrup, J. S., Pedersen, L. Ø., Buus, S., & Gajhede, M. (2006). Structure of HLA-A*1101 in complex with a hepatitis B peptide homologue. Acta Crystallographica Section F-Structural Biology and Crystallization Communications, 62(Pt 12), 1179-84. https://doi.org/10.1107/S1744309106044228

Vancouver

Blicher T, Kastrup JS, Pedersen LØ, Buus S, Gajhede M. Structure of HLA-A*1101 in complex with a hepatitis B peptide homologue. Acta Crystallographica Section F-Structural Biology and Crystallization Communications. 2006;62(Pt 12):1179-84. https://doi.org/10.1107/S1744309106044228

Author

Blicher, Thomas ; Kastrup, Jette Sandholm ; Pedersen, Lars Østergaard ; Buus, Søren ; Gajhede, Michael. / Structure of HLA-A*1101 in complex with a hepatitis B peptide homologue. In: Acta Crystallographica Section F-Structural Biology and Crystallization Communications. 2006 ; Vol. 62, No. Pt 12. pp. 1179-84.

Bibtex

@article{531609d0ebc911ddbf70000ea68e967b,
title = "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).",
author = "Thomas Blicher and Kastrup, {Jette Sandholm} and Pedersen, {Lars {\O}stergaard} and S{\o}ren Buus and Michael Gajhede",
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",
year = "2006",
doi = "10.1107/S1744309106044228",
language = "English",
volume = "62",
pages = "1179--84",
journal = "Acta Crystallographica Section F: Structural Biology Communications",
issn = "2053-230X",
publisher = "Wiley",
number = "Pt 12",

}

RIS

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

VL - 62

SP - 1179

EP - 1184

JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

SN - 2053-230X

IS - Pt 12

ER -

ID: 9942600