› 3m9e

X-ray diffraction
2.41Å resolution

Thyroid hormone beta DNA binding domain homodimer with inverted palindrome TRE

Released:
DOI: 10.2210/pdb3m9e/pdb
PDB entry 3m9e coloured by chain, front view.
PDB entry 3m9e coloured by chain, side view.
PDB entry 3m9e coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Structure of a thyroid hormone receptor DNA-binding domain homodimer bound to an inverted palindrome DNA response element.
Chen Y, Young MA
Mol Endocrinol 24 1650-64 (2010)
PMID: 20610536

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-116551 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
Macromolecules (2 distinct):
Thyroid hormone receptor beta Chains: A, B, E, F
Molecule details ›
Chains: A, B, E, F
Length: 105 amino acids
Theoretical weight: 12.33 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P18113 (Residues: 104-206; Coverage: 22%)
Gene names: Erba2, Nr1a2, Thrb
Sequence domains: Zinc finger, C4 type (two domains)
Structure domains: Erythroid Transcription Factor GATA-1, subunit A
DNA (5'-D(*AP*TP*TP*GP*AP*CP*CP*TP*CP*AP*GP*CP*TP*GP*AP*GP*GP*TP*CP*AP*AP*T)-3') Chains: C, D, G, H
Molecule details ›
Chains: C, D, G, H
Length: 22 nucleotides
Theoretical weight: 6.75 KDa
Source organism: Rattus norvegicus
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand ZN 8 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P21
Unit cell:
a: 73.738Å b: 83.468Å c: 75.743Å
α: 90° β: 98.28° γ: 90°
R-values:
R R work R free
0.19 0.179 0.231
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

4 review citations

General molecular biology and architecture of nuclear receptors.
Pawlak et al. (2012)
3 more

2 mentions without citation

A New Mechanism in THRA Resistance: The First Disease-Associated Variant Leading to an Increased Inhibitory Function of THRA2.
Paisdzior et al. (2021)
1 more