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Title: Expression, refolding and crystallization of murine MHC class I H-2D{sup b} in complex with human β{sub 2}-microglobulin

Abstract

Mouse MHC class I H-2Db in complex with human β2m and the LCMV-derived peptide gp33 has been produced and crystallized. Resolution of the structure of this complex combined with the structural comparison with the previously solved crystal structure of H-2Db/mβ2m/gp33 should lead to a better understanding of how the β2m subunit affects the overall conformation of MHC complexes as well as the stability of the presented peptides. β{sub 2}-Microglobulin (β{sub 2}m) is non-covalently linked to the major histocompatibility (MHC) class I heavy chain and interacts with CD8 and Ly49 receptors. Murine MHC class I can bind human β{sub 2}m (hβ{sub 2}m) and such hybrid molecules are often used in structural and functional studies. The replacement of mouse β{sub 2}m (mβ{sub 2}m) by hβ{sub 2}m has important functional consequences for MHC class I complex stability and specificity, but the structural basis for this is unknown. To investigate the impact of species-specific β{sub 2}m subunits on MHC class I conformation, murine MHC class I H-2D{sup b} in complex with hβ{sub 2}m and the peptide gp33 derived from lymphocytic choriomeningitis virus (LCMV) has been expressed, refolded in vitro and crystallized. Crystals containing two complexes per asymmetric unit and belonging to the space groupmore » P2{sub 1}, with unit-cell parameters a = 68.1, b = 65.2, c = 101.9 Å, β = 102.4°, were obtained.« less

Authors:
 [1];  [2];  [3];  [2];  [4];  [1];  [2]
  1. Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm (Sweden)
  2. Center for Infectious Medicine, Department of Medicine, Karolinska Institutet, Karolinska University Hospital in Huddinge, Stockholm (Sweden)
  3. Center for Molecular Medicine, Karolinska University Hospital in Solna, Karolinska Institutet, Stockholm (Sweden)
  4. Microbiology and Tumor Biology Center, Karolinska Institutet, Stockholm (Sweden)
Publication Date:
OSTI Identifier:
22356204
Resource Type:
Journal Article
Journal Name:
Acta Crystallographica. Section F
Additional Journal Information:
Journal Volume: 61; Journal Issue: Pt 12; Other Information: PMCID: PMC1978157; PMID: 16511243; PUBLISHER-ID: en5132; OAI: oai:pubmedcentral.nih.gov:1978157; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTAL STRUCTURE; CRYSTALLIZATION; CRYSTALS; HYBRIDIZATION; IN VITRO; MOLECULES; RECEPTORS; RESOLUTION; SPACE GROUPS; SPECIFICITY; STABILITY

Citation Formats

Sandalova, Tatyana, Michaëlsson, Jakob, Harris, Robert A., Ljunggren, Hans-Gustaf, Kärre, Klas, Schneider, Gunter, Achour, Adnane, and Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm. Expression, refolding and crystallization of murine MHC class I H-2D{sup b} in complex with human β{sub 2}-microglobulin. United Kingdom: N. p., 2005. Web. doi:10.1107/S1744309105037942.
Sandalova, Tatyana, Michaëlsson, Jakob, Harris, Robert A., Ljunggren, Hans-Gustaf, Kärre, Klas, Schneider, Gunter, Achour, Adnane, & Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm. Expression, refolding and crystallization of murine MHC class I H-2D{sup b} in complex with human β{sub 2}-microglobulin. United Kingdom. https://doi.org/10.1107/S1744309105037942
Sandalova, Tatyana, Michaëlsson, Jakob, Harris, Robert A., Ljunggren, Hans-Gustaf, Kärre, Klas, Schneider, Gunter, Achour, Adnane, and Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm. 2005. "Expression, refolding and crystallization of murine MHC class I H-2D{sup b} in complex with human β{sub 2}-microglobulin". United Kingdom. https://doi.org/10.1107/S1744309105037942.
@article{osti_22356204,
title = {Expression, refolding and crystallization of murine MHC class I H-2D{sup b} in complex with human β{sub 2}-microglobulin},
author = {Sandalova, Tatyana and Michaëlsson, Jakob and Harris, Robert A. and Ljunggren, Hans-Gustaf and Kärre, Klas and Schneider, Gunter and Achour, Adnane and Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm},
abstractNote = {Mouse MHC class I H-2Db in complex with human β2m and the LCMV-derived peptide gp33 has been produced and crystallized. Resolution of the structure of this complex combined with the structural comparison with the previously solved crystal structure of H-2Db/mβ2m/gp33 should lead to a better understanding of how the β2m subunit affects the overall conformation of MHC complexes as well as the stability of the presented peptides. β{sub 2}-Microglobulin (β{sub 2}m) is non-covalently linked to the major histocompatibility (MHC) class I heavy chain and interacts with CD8 and Ly49 receptors. Murine MHC class I can bind human β{sub 2}m (hβ{sub 2}m) and such hybrid molecules are often used in structural and functional studies. The replacement of mouse β{sub 2}m (mβ{sub 2}m) by hβ{sub 2}m has important functional consequences for MHC class I complex stability and specificity, but the structural basis for this is unknown. To investigate the impact of species-specific β{sub 2}m subunits on MHC class I conformation, murine MHC class I H-2D{sup b} in complex with hβ{sub 2}m and the peptide gp33 derived from lymphocytic choriomeningitis virus (LCMV) has been expressed, refolded in vitro and crystallized. Crystals containing two complexes per asymmetric unit and belonging to the space group P2{sub 1}, with unit-cell parameters a = 68.1, b = 65.2, c = 101.9 Å, β = 102.4°, were obtained.},
doi = {10.1107/S1744309105037942},
url = {https://www.osti.gov/biblio/22356204}, journal = {Acta Crystallographica. Section F},
issn = {1744-3091},
number = Pt 12,
volume = 61,
place = {United Kingdom},
year = {Thu Dec 01 00:00:00 EST 2005},
month = {Thu Dec 01 00:00:00 EST 2005}
}