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HLA-B27 subtypes differentially associated with disease exhibit conformational differences in solution.

Heinz Fabian1, Hans Huser, Daniele Narzi

  • 1Robert Koch-Institut, P 25, Nordufer 20, D-13353 Berlin, Germany. fabianh@rki.de

Journal of Molecular Biology
|January 8, 2008
PubMed
Summary

Human leukocyte antigen (HLA) B27 subtypes associated with ankylosing spondylitis exhibit increased heavy chain flexibility. This difference in flexibility, influenced by a single amino acid residue, impacts the peptide binding groove and may affect immune cell recognition.

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Area of Science:

  • Immunogenetics
  • Structural Biology
  • Biophysics

Background:

  • Human leukocyte antigen (HLA) class I molecules are crucial for immune response.
  • Specific HLA-B27 subtypes are linked to ankylosing spondylitis, differing by a single amino acid at residue 116.
  • This residue variation affects the peptide-binding groove's F pocket, influencing peptide C-terminus accommodation.

Purpose of the Study:

  • To investigate the structural and dynamic differences between HLA-B27 subtypes associated with ankylosing spondylitis (HLA-B*2705) and those not associated (HLA-B*2709).
  • To elucidate how the single amino acid difference at position 116 impacts peptide binding groove flexibility and function.

Main Methods:

  • Isotope-edited infrared (IR) spectroscopy was employed to study HLA-B27 subtypes complexed with a self-peptide.
  • Molecular dynamics simulations were performed to analyze the flexibility and dynamics of the peptide binding groove.

Main Results:

  • Isotope-edited IR spectroscopy revealed greater heavy chain flexibility in HLA-B*2705 compared to HLA-B*2709.
  • Molecular dynamics simulations confirmed increased binding groove flexibility in HLA-B*2705.
  • This enhanced flexibility correlates with an opening of the HLA-B*2705 binding groove and partial detachment of the peptide C-terminal anchor.

Conclusions:

  • A single polymorphic residue (116) in the HLA-B27 heavy chain significantly influences peptide binding groove flexibility in a subtype-dependent manner.
  • These dynamic differences may play a role in the recognition of HLA-B27 complexes by immune effector cells, potentially explaining disease association.
  • The findings highlight the subtle structural variations that can have profound functional and immunological consequences.