› 2fbr

X-ray diffraction
1.46Å resolution

Human transthyretin (TTR) complexed with bivalant amyloid inhibitor (4 carbon linker)

Released:
DOI: 10.2210/pdb2fbr/pdb
PDB 2fbr coloured by chain and viewed from the front.
PDB 2fbr coloured by chain and viewed from the side.
PDB 2fbr coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Synthesis and characterization of potent bivalent amyloidosis inhibitors that bind prior to transthyretin tetramerization.
Green NS, Palaninathan SK, Sacchettini JC, Kelly JW
J. Am. Chem. Soc. 125 13404-14 (2003)
PMID: 14583036

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (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 44C 1 x 44C
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P21212
Unit cell:
a: 42.599Å b: 84.355Å c: 65.569Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.21 0.224
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Review on the Structures and Activities of Transthyretin Amyloidogenesis Inhibitors.
Guo et al. (2020)
8 more

7 mentions without citation

Toward optimization of the linker substructure common to transthyretin amyloidogenesis inhibitors using biochemical and structural studies.
Johnson et al. (2008)
6 more