› 1ld9

X-ray diffraction
2.4Å resolution

THE THREE-DIMENSIONAL STRUCTURE OF AN H-2LD PEPTIDE COMPLEX EXPLAINS THE UNIQUE INTERACTION OF LD WITH BETA2M AND PEPTIDE

Released:
DOI: 10.2210/pdb1ld9/pdb
PDB entry 1ld9 coloured by chain, front view.
PDB entry 1ld9 coloured by chain, side view.
PDB entry 1ld9 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
The three-dimensional structure of an H-2Ld-peptide complex explains the unique interaction of Ld with beta-2 microglobulin and peptide.
Balendiran GK, Solheim JC, Young AC, Hansen TH, Nathenson SG, Sacchettini JC
Proc Natl Acad Sci U S A 94 6880-5 (1997)
PMID: 9192660

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
H-2 class I histocompatibility antigen, L-D alpha chain Chains: A, D
Molecule details ›
Chains: A, D
Length: 268 amino acids
Theoretical weight: 30.96 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P01897 (Residues: 25-292; Coverage: 79%)
Gene name: H2-L
Sequence domains:
Structure domains:
Beta-2-microglobulin Chains: B, E
Molecule details ›
Chains: B, E
Length: 99 amino acids
Theoretical weight: 11.7 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P01887 (Residues: 21-119; Coverage: 100%)
Gene name: B2m
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins
NANO-PEPTIDE Chains: C, F
Molecule details ›
Chains: C, F
Length: 9 amino acids
Theoretical weight: 1.12 KDa

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P21212
Unit cell:
a: 150.1Å b: 87.2Å c: 80.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.186 0.279
Expression system: Escherichia coli

Quick links

Citations

8 review citations

MHC superfamily structure and the immune system.
Maenaka et al. (1999)
7 more

16 mentions without citation

Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3.
Wang et al. (2007)
15 more