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

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

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

Published Date

  • January 14, 1994

Published In

Volume / Issue

  • 76 / 1

Start / End Page

  • 39 - 50

PubMed ID

  • 7506996

International Standard Serial Number (ISSN)

  • 0092-8674

Digital Object Identifier (DOI)

  • 10.1016/0092-8674(94)90171-6


  • eng

Conference Location

  • United States