1hoc
THE THREE-DIMENSIONAL STRUCTURE OF H-2DB AT 2.4 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ANTIGEN-DETERMINANT SELECTION
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OverviewOverview
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.
About this StructureAbout this Structure
1HOC is a Protein complex structure of sequences from Influenza a virus and Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
The three-dimensional structure of H-2Db at 2.4 A resolution: implications for antigen-determinant selection., Young AC, Zhang W, Sacchettini JC, Nathenson SG, Cell. 1994 Jan 14;76(1):39-50. PMID:7506996
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