› 3ipe

X-ray diffraction
1.4Å resolution

Human Transthyretin (TTR) complexed with a palindromic bivalent amyloid inhibitor (7 carbon linker).

Released:
DOI: 10.2210/pdb3ipe/pdb
PDB entry 3ipe coloured by chain, front view.
PDB entry 3ipe coloured by chain, side view.
PDB entry 3ipe coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Trapping of palindromic ligands within native transthyretin prevents amyloid formation.
Kolstoe SE, Mangione PP, Bellotti V, Taylor GW, Tennent GA, Deroo S, Morrison AJ, Cobb AJ, Coyne A, McCammon MG, Warner TD, Mitchell J, Gill R, Smith MD, Ley SV, Robinson CV, Wood SP, Pepys MB
Proc Natl Acad Sci U S A 107 20483-8 (2010)
PMID: 21059958

Function and Biology Details

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

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: 13.78 KDa
Source organism: Homo sapiens
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 JZE 1 x JZE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21212
Unit cell:
a: 43.241Å b: 84.876Å c: 63.39Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.175 0.196

Quick links

Citations

11 review citations

The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug.
Johnson et al. (2012)
10 more

6 mentions without citation

Targeting Amyloid Aggregation: An Overview of Strategies and Mechanisms.
Giorgetti et al. (2018)
5 more