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Related Concept Videos

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Related Experiment Video

Updated: Feb 21, 2026

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
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Direct evidence for conformational dynamics in major histocompatibility complex class I molecules.

Andy van Hateren1, Malcolm Anderson2, Alistair Bailey3

  • 1Institute for Life Sciences and Centre for Cancer Immunology, Faculty of Medicine, Southampton SO17 1BJ.

The Journal of Biological Chemistry
|October 13, 2017
PubMed
Summary

Major histocompatibility complex class I (MHC I) molecules exhibit dynamic conformational changes, revealing a mechanism for peptide selection crucial for immune responses. This MHC I plasticity influences how effectively peptides are presented to T lymphocytes.

Keywords:
allotypeantigen presentationhydrogen–deuterium exchangehydrogen–deuterium exchange mass spectrometrymajor histocompatibility complex (MHC)protein conformationprotein dynamicprotein foldingprotein structurestructure-function

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Area of Science:

  • Immunology
  • Structural Biology
  • Molecular Biology

Background:

  • Major histocompatibility complex class I (MHC I) molecules present peptides to cytotoxic T lymphocytes, a critical step in adaptive immunity.
  • MHC I molecules exhibit peptide specificity, but the underlying selection mechanism and molecular basis for this discrimination remain largely unknown.
  • The dynamic nature and conformational plasticity of MHC I molecules are hypothesized to be involved in peptide selection but have been difficult to study due to instability.

Purpose of the Study:

  • To investigate the dynamic conformational changes of MHC I molecules.
  • To elucidate the mechanism by which MHC I molecules select specific peptides for presentation.
  • To understand the role of MHC I plasticity in peptide binding and antigen presentation.

Main Methods:

  • Refolding of MHC I proteins with UV-light-cleavable peptides.
  • Comparison of peptide-loaded MHC I with peptide-receptive MHC I using hydrogen-deuterium exchange mass spectrometry (HDX-MS).
  • Analysis of deuterium exchange in different MHC I domains and associated β2-microglobulin across various allotypes.

Main Results:

  • Significant differences in hydrogen-deuterium exchange were observed between peptide-loaded and peptide-receptive MHC I molecules.
  • UV-induced peptide hydrolysis led to increased deuterium exchange in the peptide-binding domain and other regions, indicating long-range conformational changes.
  • Allotype-specific differences in hydrogen-deuterium exchange patterns were detected, supporting the role of MHC I plasticity in peptide selection.

Conclusions:

  • MHC I molecules possess inherent dynamic conformational plasticity that is modulated by peptide binding.
  • This conformational plasticity is a key factor in the selective binding and presentation of peptides, influencing immune recognition.
  • Understanding MHC I dynamics offers potential for developing novel immune-modulatory therapies.