1HOC

THE THREE-DIMENSIONAL STRUCTURE OF H-2DB AT 2.4 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ANTIGEN-DETERMINANT SELECTION

Summary for 1HOC

• Entry DOI: 10.2210/pdb1hoc/pdb
• Descriptor: CLASS I HISTOCOMPATIBILITY ANTIGEN (H2-DB) (ALPHA CHAIN), BETA 2-MICROGLOBULIN, 9-RESIDUE PEPTIDE, ... (4 entities in total)
• Functional Keywords: histocompatibility antigen
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 3
• Total formula weight: 44248.53

Authors

Young, A.C.M.,Zhang, W.,Sacchettini, J.C. (deposition date: 1994-01-02, release date: 1994-04-30, Last modification date: 2024-10-23)

Primary citation

Young, A.C.,Zhang, W.,Sacchettini, J.C.,Nathenson, S.G.
The three-dimensional structure of H-2Db at 2.4 A resolution: implications for antigen-determinant selection
Cell(Cambridge,Mass.), 76:39-50, 1994

PubMed 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.

PubMed: 7506996
DOI: 10.1016/0092-8674(94)90171-6

Experimental method

X-RAY DIFFRACTION (2.4 Å)