The interface between tapasin and MHC class I: Identification of amino acid residues in both proteins that influence their interaction

Hēth R. Turnquist, Shanna E. Vargas, Erin L. Schenk, Mary M. McIlhaney, Adrian J. Reber, Joyce C. Solheim

Research output: Contribution to journalReview articlepeer-review

22 Scopus citations

Abstract

Prior to the binding of antigenic peptide, a complex of chaperone proteins associates with the Major Histocompatibility Complex (MHC) class I heavy chain/β2m heterodimer. Although each domain of the MHC class I heavy chain contains amino acid residues that influence chaperone binding, there are several pieces of evidence that point to an interaction between the MHC class I α2/α3 domains and tapasin. In regard to the site on tapasin involved in the tapasin/MHC interface, we have found that a particular region of tapasin (containing amino acid residues 334-342) is necessary for the binding of tapasin to the MHC class I heavy chain. Our results also indicate that amino acids in this region of tapasin also affect the proportion of MHC class I open forms expressed at the cell surface and MHC class I egress from the endoplasmic reticulum. Based on these results and those obtained by other laboratories, a model for MHC class I/tapasin interaction is proposed.

Original languageEnglish (US)
Pages (from-to)261-269
Number of pages9
JournalImmunologic Research
Volume25
Issue number3
DOIs
StatePublished - 2002

Keywords

  • Antigen presentation
  • Chaperone
  • Major histocompatibility complex class I
  • Tapasin
  • Transporter associated with antigen processing

ASJC Scopus subject areas

  • Immunology

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