› 1tvh

X-ray diffraction
1.8Å resolution

Crystal structure of Modified Melanoma Antigen gp100(209-T2M) Bound to Human Class I MHC HLA-A2

Released:
DOI: 10.2210/pdb1tvh/pdb
PDB entry 1tvh coloured by chain, front view.
PDB entry 1tvh coloured by chain, side view.
PDB entry 1tvh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Increased immunogenicity of an anchor-modified tumor-associated antigen is due to the enhanced stability of the peptide/MHC complex: implications for vaccine design.
Borbulevych OY, Baxter TK, Yu Z, Restifo NP, Baker BM
J Immunol 174 4812-20 (2005)
PMID: 15814707

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-137690 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
HLA class I histocompatibility antigen, A alpha chain Chains: A, D
Molecule details ›
Chains: A, D
Length: 275 amino acids
Theoretical weight: 31.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P04439 (Residues: 25-299; Coverage: 81%)
Gene names: HLA-A, HLAA
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
M-alpha Chains: C, F
Molecule details ›
Chains: C, F
Length: 9 amino acids
Theoretical weight: 1.04 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P40967 (Residues: 209-217; Coverage: 1%)
Gene names: D12S53E, PMEL, PMEL17, SILV

Ligands and Environments

1 bound ligand:
Ligand GOL 28 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P21
Unit cell:
a: 58.407Å b: 84.485Å c: 84.014Å
α: 90° β: 90.11° γ: 90°
R-values:
R R work R free
0.188 0.185 0.247
Expression systems:
  • Escherichia coli BL21
  • Escherichia coli
  • Not provided

Quick links

Citations

19 review citations

Translating tumor antigens into cancer vaccines.
Buonaguro et al. (2011)
18 more

9 mentions without citation

Increased immunogenicity of an anchor-modified tumor-associated antigen is due to the enhanced stability of the peptide/MHC complex: implications for vaccine design.
Borbulevych et al. (2005)
8 more