Loss of a glycine in the α2 domain affects MHC peptide binding but not chaperone binding

Heth R. Turnquist, Shanna E. Vargas, Joyce C. Solheim

Research output: Contribution to journalArticlepeer-review

1 Scopus citations


Prior to the binding of peptide in the endoplasmic reticulum (ER), the major histocompatibility complex (MHC) class I heavy chain associates with an assembly complex that includes the transporter associated with antigen processing (TAP). The proximity of a part of the MHC class I α2 domain α-helix to areas previously shown to influence assembly complex binding suggests that this region might also be involved in chaperone association. Position 151, found in this part of the α2 domain α-helix, has a side chain that points up, away from direct contact with peptide, and is occupied by a glycine in all murine MHC class I heavy chains. We found that substitution of this glycine in H-2Ld with a histidine substantially increased the proportion of peptide-free forms, although TAP binding was not abrogated. Thus, interaction of the heavy chain with peptides, but not with the assembly complex, is influenced by this glycine.

Original languageEnglish (US)
Pages (from-to)825-831
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number4
StatePublished - Dec 14 2001


  • Antigen presentation
  • Assembly complex
  • Chaperone
  • Major histocompatibility complex
  • Transporter associated with antigen processing

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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