H2-M3, a full-service class Ib histocompatibility antigen

Kirsten Fischer Lindahl, Derek E. Byers, Vikram M. Dabhi, Rolf Hovik, Elsy P. Jones, Geoffrey P. Smith, Chyung Ru Wang, Hong Xiao, Masayasu Yoshino

Research output: Contribution to journalReview articlepeer-review

113 Scopus citations


H2-M3 is an MHC class Ib molecule of the mouse with a unique preference for N-formylated peptides, which may come from the N-termini of endogenous, mitochondrial proteins or foreign, bacterial proteins. The crystal structure of M3 revealed a hydrophobic peptide-binding groove with an occluded A pocket and the peptide shifted one residue relative to class la structures. The formyl group is held by a novel hydrogen bonding network, involving His9 on the bottom of the groove, and the side chain of the P 1 methionine is lodged in the B pocket. M3 is a full-service histocompatibility (H) antigen, i.e. self-M3 can present endogenous peptides as minor H antigens and foreign, bacterial antigens in a defensive immune response to infection: and foreign M3 complexed with endogenous self-peptides can be recognized as an alloantigen. The hydrophobic groove of M3 may also allow it to present nonpeptide ligands in the manner of human CD1.

Original languageEnglish
Pages (from-to)851-879
Number of pages29
JournalAnnual Review of Immunology
StatePublished - 1997


  • Listeria
  • antigen presentation
  • crystal structure
  • formyl-methionine
  • major histocompatibility complex


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