Crystal structure of mouse H2-M

Immunity. 1998 Sep;9(3):385-93. doi: 10.1016/s1074-7613(00)80621-4.

Abstract

H2-M (HLA-DM in humans) resides in an acidic endosomal compartment, where it facilitates the loading of antigenic peptides into the peptide-binding groove of class II MHC. The crystal structure of a soluble form of H2-M has been solved to 3.1 A resolution, revealing a heterodimer with structural similarities to the MHC family of proteins. In contrast to its antigen-presenting cousins, the membrane distal alpha helices of H2-M pack closely together, occluding most of the binding groove except for a single large pocket near the center. The structure of H2-M has several unique features that may play a role in its function as a molecular chaperone and peptide exchange factor.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Conserved Sequence
  • Crystallography, X-Ray
  • HLA-D Antigens / chemistry*
  • HLA-D Antigens / isolation & purification
  • HLA-D Antigens / physiology
  • Histocompatibility Antigens Class I / chemistry
  • Histocompatibility Antigens Class II / chemistry
  • Mice
  • Mice, Inbred C57BL
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Structure, Tertiary
  • Solubility

Substances

  • H2-M antigens
  • HLA-D Antigens
  • HLA-DM antigens
  • Histocompatibility Antigens Class I
  • Histocompatibility Antigens Class II

Associated data

  • PDB/1H2M
  • PDB/1IEA