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Role of chain pairing for the production of functional soluble IA major histocompatibility complex class II molecules

Academic Article
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Overview

related to degree

  • Scott, Christopher, Ph.D. in Biology, Scripps Research 1993 - 1998

authors

  • Scott, Christopher
  • Garcia, K. C.
  • Carbone, F. R.
  • Wilson, Ian
  • Teyton, Luc

publication date

  • 1996

journal

  • Journal of Experimental Medicine  Journal

abstract

  • Structural studies of cellular receptor molecules involved in immune recognition require the production of large quantities of the extracellular domains of these glycoproteins. The murine major histocompatibility complex (MHC) class II-restricted response has been extensively studied by functional means, but the engineering and purification of the native, empty form of the most-studied murine MHC class II molecule, IA, has been difficult to achieve. IA molecules, which are the murine equivalent of human histocompatibility leukocyte antigen-DQ molecules, have a low efficiency of chain pairing, which results in poor transport to the cell surface and in the appearance of mixed isotype pairs. We have engineered soluble IA molecules whose pairing has been forced by the addition of leucine zipper peptide dimers at their COOH-terminus. The molecules are secreted "empty" into the extracellular medium and can be loaded with single peptide after purification. These IA molecules have been expressed in milligram quantity for crystallization as well as for activation of T cells and measurement of MHC class II-T cell receptor interactions.

subject areas

  • Amino Acid Sequence
  • Animals
  • Cell Line
  • Cells, Cultured
  • DNA Primers
  • DNA, Complementary
  • Drosophila melanogaster
  • HLA-DQ Antigens
  • Histocompatibility Antigens Class II
  • Humans
  • Kinetics
  • Leucine Zippers
  • Mice
  • Molecular Sequence Data
  • Polymerase Chain Reaction
  • Receptors, Antigen, T-Cell
  • Recombinant Proteins
  • T-Lymphocytes
  • Thrombin
  • Transfection
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Identity

PubMed Central ID

  • PMC2192579

International Standard Serial Number (ISSN)

  • 0022-1007

Digital Object Identifier (DOI)

  • 10.1084/jem.183.5.2087

PubMed ID

  • 8642319
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Additional Document Info

start page

  • 2087

end page

  • 2095

volume

  • 183

issue

  • 5

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