› 2f74

X-ray diffraction
2.7Å resolution

Murine MHC class I H-2Db in complex with human b2-microglobulin and LCMV-derived immunodminant peptide gp33

Released:
DOI: 10.2210/pdb2f74/pdb
PDB entry 2f74 coloured by chain, front view.
PDB entry 2f74 coloured by chain, side view.
PDB entry 2f74 coloured by chain, top view.
Source organisms:
Primary publication:
Structural basis of the differential stability and receptor specificity of H-2Db in complex with murine versus human beta2-microglobulin.
Achour A, Michaëlsson J, Harris RA, Ljunggren HG, Kärre K, Schneider G, Sandalova T
J Mol Biol 356 382-96 (2006)
PMID: 16375919

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-135289 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
H-2 class I histocompatibility antigen, D-B alpha chain Chains: A, D
Molecule details ›
Chains: A, D
Length: 276 amino acids
Theoretical weight: 32.09 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P01899 (Residues: 25-300; Coverage: 82%)
Gene name: H2-D1
Sequence domains:
Structure domains:
Beta-2-microglobulin Chains: B, E
Molecule details ›
Chains: B, E
Length: 100 amino acids
Theoretical weight: 11.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P61769 (Residues: 21-119; Coverage: 100%)
Gene names: B2M, CDABP0092, HDCMA22P
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins
NONAMERIC PEPTIDE, GP33, DERIVED FROM LYMPHOCYTIC CHORIOMENINGITIS VIRUS Chains: C, F
Molecule details ›
Chains: C, F
Length: 9 amino acids
Theoretical weight: 1.05 KDa

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P21
Unit cell:
a: 68.142Å b: 65.197Å c: 101.941Å
α: 90° β: 102.43° γ: 90°
R-values:
R R work R free
0.227 0.223 0.298
Expression system: Escherichia coli

Quick links

Citations

21 citation in other articles

Structure of the TAPBPR-MHC I complex defines the mechanism of peptide loading and editing.
Thomas et al. (2017)
20 more

2 mentions without citation

Structural allele-specific patterns adopted by epitopes in the MHC-I cleft and reconstruction of MHC:peptide complexes to cross-reactivity assessment.
Antunes et al. (2010)
1 more