The three-dimensional structure of H-2Db at 2.4 A resolution: implications for antigen-determinant selection. Academic Article uri icon


  • Solution at 2.4 A resolution of the structure of H-2Db with the influenza virus peptide NP366-374 (ASNEN-METM) and comparison with the H-2Kb-VSV (RGY-VYQGL) structure allow description of the molecular details of MHC class I peptide binding interactions for mice of the H-2b haplotype, revealing a strategy that maximizes the repertoire of peptides than can be presented. The H-2Db cleft has a mouse-specific hydrophobic ridge that causes a compensatory arch in the backbone of the peptide, exposing the arch residues to TCR contact and requiring the peptide to be at least 9 residues. This ridge occurs in about 40% of the known murine D and L allelic molecules, classifying them as a structural subgroup.

published proceedings

  • Cell

author list (cited authors)

  • Young, A. C., Zhang, W., Sacchettini, J. C., & Nathenson, S. G.

citation count

  • 217

complete list of authors

  • Young, AC||Zhang, W||Sacchettini, JC||Nathenson, SG

publication date

  • January 1994

published in