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

abstract

• 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.

authors

• Sacchettini, James

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

publisher

• Elsevier  Publisher

published in

• Cell  Journal

keywords

• Amino Acid Sequence
• Animals
• Base Sequence
• Binding Sites
• Cloning, Molecular
• Epitopes
• H-2 Antigens
• Histocompatibility Antigen H-2d
• Hydrogen Bonding
• Mice
• Models, Molecular
• Molecular Sequence Data
• Oligodeoxyribonucleotides
• Polymerase Chain Reaction
• Protein Conformation
• Protein Structure, Secondary
• Receptors, Antigen, T-Cell
• Recombinant Proteins
• X-Ray Diffraction

PubMed Central ID

• 7506996

Digital Object Identifier (DOI)

• 10.1016/0092-8674(94)90171-6

start page

• 39

end page

• 50

volume

• 76

issue

• 1