Conformational changes induced in the MHC class I molecule by peptide and β2-microglobulin

Joyce C. Solheim, James R. Cook, Ted H. Hansen

Research output: Contribution to journalArticlepeer-review

7 Scopus citations


Assembly of the class I MHC molecule is inextricably linked to the antigen presentation function of the class I molecule. Association of the class I MHC molecule with β2-microglobulin (β2m) is a prerequisite for association with the heterodimeric protein TAP, and once peptide is acquired, the class I molecule folds and begins its sojourn to the cell surface. To maintain its folded conformation, class I MHC requires peptide but not β2m, and the sequence of the peptide bound exercises a subtle influence on the structure of the class I molecule that is likely to be a factor in T cell receptor discrimination of MHC/peptide complexes.

Original languageEnglish (US)
Pages (from-to)200-217
Number of pages18
JournalImmunologic Research
Issue number3
StatePublished - Sep 1995
Externally publishedYes


  • Conformation
  • Major histocompatibility complex
  • Peptide
  • β-microglobulin

ASJC Scopus subject areas

  • Immunology


Dive into the research topics of 'Conformational changes induced in the MHC class I molecule by peptide and β<sub>2</sub>-microglobulin'. Together they form a unique fingerprint.

Cite this