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Crystal structure of mouse H2-M

D H Fremont1, F Crawford, P Marrack

  • 1Center for Immunology, Department of Pathology, Washington University School of Medicine, St. Louis, Missouri 63110, USA. fremont@immunology.wustl.edu

Immunity
|October 13, 1998
PubMed
Summary

The crystal structure of H2-M (human HLA-DM) reveals unique features that explain its role in loading peptides onto MHC class II molecules for immune response.

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Area of Science:

  • Immunology
  • Structural Biology
  • Molecular Biology

Background:

  • H2-M (human HLA-DM) is crucial for antigen presentation.
  • It functions in acidic endosomes to load peptides onto MHC class II molecules.

Purpose of the Study:

  • To determine the crystal structure of a soluble form of H2-M.
  • To elucidate the structural basis for H2-M's function as a molecular chaperone and peptide exchange factor.

Main Methods:

  • X-ray crystallography was used to solve the crystal structure of H2-M.
  • The structure was determined at 3.1 A resolution.

Main Results:

  • H2-M forms a heterodimer with structural similarities to MHC proteins.
  • Unique structural features include closely packed alpha helices occluding the binding groove, except for a central pocket.

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Conclusions:

  • The solved structure provides insights into H2-M's mechanism of action.
  • Unique structural characteristics likely facilitate its role in peptide loading and exchange for MHC class II.