› 3kgu

X-ray diffraction
1.85Å resolution

Wild type human transthyretin (TTR) complexed with genistein (TTRwt:GEN) pH 7.5

Released:
DOI: 10.2210/pdb3kgu/pdb
PDB entry 3kgu coloured by chain, front view.
PDB entry 3kgu coloured by chain, side view.
PDB entry 3kgu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Conformational differences between the wild type and V30M mutant transthyretin modulate its binding to genistein: implications to tetramer stability and ligand-binding.
Trivella DB, Bleicher L, Palmieri Lde C, Wiggers HJ, Montanari CA, Kelly JW, Lima LM, Foguel D, Polikarpov I
J Struct Biol 170 522-31 (2010)
PMID: 20211733

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
Expression system: Escherichia coli
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 GEN 2 x GEN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE W01B-MX2
Spacegroup: P21212
Unit cell:
a: 43.53Å b: 85.35Å c: 64.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.197 0.234
Expression system: Escherichia coli

Quick links

Citations

6 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)
5 more

1 mention without citation

Substoichiometric inhibition of transthyretin misfolding by immune-targeting sparsely populated misfolding intermediates: a potential diagnostic and therapeutic for TTR amyloidoses.
Galant et al. (2016)