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Human class II MHC molecule HLA-DR1: X-ray structure determined from three crystal forms.

J H Brown1, T S Jardetzky, L J Stern

  • 1Department of Biochemistry and Molecular Biology, Howard Hughes Medical Institute, Harvard University, Cambridge, MA 02138, USA.

Acta Crystallographica. Section D, Biological Crystallography
|November 1, 1995
PubMed
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The three-dimensional structure of human leukocyte antigen DR1 (HLA-DR1) was determined using X-ray crystallography. This reveals the molecular interactions of HLA-DR1 with peptides and superantigens.

Area of Science:

  • Structural Biology
  • Immunology
  • Biochemistry

Background:

  • Major histocompatibility complex (MHC) class II molecules present peptides to T cells, playing a crucial role in immune responses.
  • Human leukocyte antigen DR1 (HLA-DR1) is a key MHC class II molecule involved in antigen presentation.
  • Understanding the three-dimensional structure of HLA-DR1 is essential for deciphering its function in immune recognition.

Purpose of the Study:

  • To determine the high-resolution three-dimensional structure of the extracellular region of HLA-DR1.
  • To investigate the structural basis of HLA-DR1 complex formation with peptides and superantigens.
  • To elucidate the molecular interactions governing antigen presentation by HLA-DR1.

Main Methods:

  • X-ray crystallography was employed to determine the structure of HLA-DR1 using three different crystal forms.

Related Experiment Videos

  • Phasing techniques, including single-isomorphous replacement, were used to generate electron-density maps.
  • Non-crystallographic real-space averaging and synchrotron radiation were utilized to achieve a 3.3 A resolution structure.

    • Main Results:

    • The three-dimensional structure of the extracellular region of HLA-DR1 was determined at 3.3 A resolution.
    • The structure revealed the binding of endogenous peptides and Staphylococcus aureus enterotoxin B (SEB) to HLA-DR1.
    • A parallel dimer of the DR1 alpha-beta heterodimer was observed in the crystal structures.

    Conclusions:

    • The determined structure provides detailed insights into the molecular architecture of HLA-DR1.
    • This structural information facilitates understanding of how HLA-DR1 interacts with various ligands, including peptides and superantigens.
    • The findings contribute to the comprehension of T cell recognition and immune system regulation.