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 journalArticle

7 Citations (Scopus)

Abstract

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
Volume14
Issue number3
DOIs
StatePublished - Sep 1 1995

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trypsinogen activation peptide
Peptides
Antigen Presentation
T-Cell Antigen Receptor
Proteins

Keywords

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

ASJC Scopus subject areas

  • Immunology

Cite this

Conformational changes induced in the MHC class I molecule by peptide and β2-microglobulin. / Solheim, Joyce C.; Cook, James R.; Hansen, Ted H.

In: Immunologic Research, Vol. 14, No. 3, 01.09.1995, p. 200-217.

Research output: Contribution to journalArticle

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