› 2qpf

X-ray diffraction
2.05Å resolution

Crystal Structure of Mouse Transthyretin

Released:
DOI: 10.2210/pdb2qpf/pdb
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PDB entry 2qpf coloured by chain, front view.
PDB entry 2qpf coloured by chain, side view.
PDB entry 2qpf coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Human-murine transthyretin heterotetramers are kinetically stable and non-amyloidogenic. A lesson in the generation of transgenic models of diseases involving oligomeric proteins.
Reixach N, Foss TR, Santelli E, Pascual J, Kelly JW, Buxbaum JN
J Biol Chem 283 2098-107 (2008)
PMID: 18006495

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-139496 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transthyretin Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 128 amino acids
Theoretical weight: 13.84 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P07309 (Residues: 21-147; Coverage: 100%)
Gene name: Ttr
Sequence domains: HIUase/Transthyretin family
Structure domains: Transthyretin/hydroxyisourate hydrolase domain

Ligands and Environments

No bound ligands
1 modified residue:
Ligand OCS 8 x OCS

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ DW
Spacegroup: P3121
Unit cell:
a: 120.511Å b: 120.511Å c: 113.186Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 0.198 0.246
Expression system: Escherichia coli

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Citations

6 review citations

Evolutionary changes to transthyretin: structure-function relationships.
Prapunpoj et al. (2009)
5 more

1 mention without citation

N-glycosylation Triggers a Dual Selection Pressure in Eukaryotic Secretory Proteins.
Medus et al. (2017)

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