› 1bzd

X-ray diffraction
1.9Å resolution

TERTIARY STRUCTURES OF THREE AMYLOIDOGENIC TRANSTHYRETIN VARIANTS AND IMPLICATIONS FOR AMYLOID FIBRIL FORMATION

Released:
DOI: 10.2210/pdb1bzd/pdb
PDB entry 1bzd coloured by chain, front view.
PDB entry 1bzd coloured by chain, side view.
PDB entry 1bzd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Tertiary structures of amyloidogenic and non-amyloidogenic transthyretin variants: new model for amyloid fibril formation.
Schormann N, Murrell JR, Benson MD
Amyloid 5 175-87 (1998)
PMID: 9818054

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: 13.81 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21212
Unit cell:
a: 43.4Å b: 86.12Å c: 65.48Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.188 0.265
Expression system: Escherichia coli

Quick links

Citations

4 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)
3 more

4 mentions without citation

Restricted mobility of conserved residues in protein-protein interfaces in molecular simulations.
Yogurtcu et al. (2008)
3 more