Analysis of the Structure of Empty and Peptide-loaded Major Histocompatibility Complex Molecules at the Cell Surface

Branimir Čatipovć, Giridhar Talluri, Joseph Oh, Taiyin Wei, Xiao Min Su, Teit E. Johansen, Michael Edidin, Jonathan P. Schneck

Research output: Contribution to journalArticlepeer-review

Abstract

We compared the conformation of empty and peptide-loaded class I major histocompatihility complex (MHC) molecules at the cell surface. Molecular conformations were analyzed by fluorescence resonance energy transfer (FRET) between fluorescent-labeled Fab fragments bound to the α2 domain of the MHC heavy chain and fluorescent-labeled Fab fragments bound to β2-microglobulin. No FRET was found between Fab fragments bound to empty H-2Kb, but FRET was detected when empty H-2Kb molecules were loaded with peptide. The magnitude of FRET depended on the sequence of the peptide used. The results imply that empty H-2Kb molecules are in a relatively extended conformation, and that this conformation becomes more compact when peptide is bound. These changes, which are reflected in peptide-dependent binding of monoclonal antibodies, affect the surfaces of MHC molecules available for contact with T cell receptors and hence may influence T cell-receptor recognition of MHC molecules.

Original languageEnglish (US)
Pages (from-to)1753-1761
Number of pages9
JournalJournal of Experimental Medicine
Volume180
Issue number5
DOIs
StatePublished - Nov 1 1994

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

Fingerprint

Dive into the research topics of 'Analysis of the Structure of Empty and Peptide-loaded Major Histocompatibility Complex Molecules at the Cell Surface'. Together they form a unique fingerprint.

Cite this