› 1ijn

X-ray diffraction
1.7Å resolution

Crystal structure of the transthyretin mutant TTR C10A/Y114C

Released:
DOI: 10.2210/pdb1ijn/pdb
PDB entry 1ijn coloured by chain, front view.
PDB entry 1ijn coloured by chain, side view.
PDB entry 1ijn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Cys114-linked dimers of transthyretin are compatible with amyloid formation.
Karlsson A, Olofsson A, Eneqvist T, Sauer-Eriksson AE
Biochemistry 44 13063-70 (2005)
PMID: 16185074

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136167 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transthyretin Chains: A, B
Molecule details ›
Chains: A, B
Length: 127 amino acids
Theoretical weight: 13.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P02766 (Residues: 21-147; Coverage: 100%)
Gene names: PALB, TTR
Sequence domains: HIUase/Transthyretin family
Structure domains: Transthyretin/hydroxyisourate hydrolase domain

Ligands and Environments

1 bound ligand:
Ligand BME 6 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P21212
Unit cell:
a: 43.15Å b: 85.235Å c: 64.797Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.204 0.237
Expression system: Escherichia coli BL21

Quick links

Citations

7 citation in other articles

Transthyretin is dysregulated in preeclampsia, and its native form prevents the onset of disease in a preclinical mouse model.
Kalkunte et al. (2013)
6 more

1 mention without citation

Impact of structural prior knowledge in SNV prediction: Towards causal variant finding in rare disease.
Dehiya et al. (2018)