› 1qwh

X-ray diffraction
1.36Å resolution

a covalent dimer of transthyretin that affects the amyloid pathway

Released:
DOI: 10.2210/pdb1qwh/pdb
PDB entry 1qwh coloured by chain, front view.
PDB entry 1qwh coloured by chain, side view.
PDB entry 1qwh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Kinetic stabilization of the native state by protein engineering: implications for inhibition of transthyretin amyloidogenesis.
Foss TR, Kelker MS, Wiseman RL, Wilson IA, Kelly JW
J Mol Biol 347 841-54 (2005)
PMID: 15769474

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: 117 amino acids
Theoretical weight: 12.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P02766 (Residues: 31-147; Coverage: 92%)
Gene names: PALB, TTR
Sequence domains: HIUase/Transthyretin family
Structure domains: Transthyretin/hydroxyisourate hydrolase domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P21212
Unit cell:
a: 43.63Å b: 86.05Å c: 63.83Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.215 0.222
Expression system: Escherichia coli BL21(DE3)

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

Linkers in the structural biology of protein-protein interactions.
Reddy Chichili et al. (2013)