1hoc
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| , resolution 2.4Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE THREE-DIMENSIONAL STRUCTURE OF H-2DB AT 2.4 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ANTIGEN-DETERMINANT SELECTION
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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