› 1iik

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF THE TRANSTHYRETIN MUTANT TTR Y114C-DATA COLLECTED AT CRYO TEMPERATURE

Released:
DOI: 10.2210/pdb1iik/pdb
PDB entry 1iik coloured by chain, front view.
PDB entry 1iik coloured by chain, side view.
PDB entry 1iik coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Disulfide-bond formation in the transthyretin mutant Y114C prevents amyloid fibril formation in vivo and in vitro.
Eneqvist T, Olofsson A, Ando Y, Miyakawa T, Katsuragi S, Jass J, Lundgren E, Sauer-Eriksson AE
Biochemistry 41 13143-51 (2002)
PMID: 12403615

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136168 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transthyretin Chains: A, B
Molecule details ›
Chains: A, B
Length: 127 amino acids
Theoretical weight: 13.72 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: ENRAF-NONIUS
Spacegroup: P21212
Unit cell:
a: 43.288Å b: 85.288Å c: 64.781Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.192 0.239
Expression system: Escherichia coli BL21

Quick links

Citations

7 citation in other articles

Amyloid fibrils containing fragmented ATTR may be the standard fibril composition in ATTR amyloidosis.
Ihse et al. (2013)
6 more

1 mention without citation

Stretching to understand proteins - a survey of the protein data bank.
SuĊ‚kowska et al. (2008)