The three-dimensional structure of H-2Db at 2.4 Å resolution: Implications for antigen-determinant selection
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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.
author list (cited authors)
Young, A., Zhang, W., Sacchettini, J. C., & Nathenson, S. G.
complete list of authors
Young, AC||Zhang, W||Sacchettini, JC||Nathenson, SG