› 4pxm

X-ray diffraction
1.9Å resolution

The Estrogen Receptor Alpha Ligand Binding Domain D538G Mutant in Complex with Estradiol and a glucocorticoid receptor-interacting protein 1 NR box II peptide

Released:
DOI: 10.2210/pdb4pxm/pdb
PDB entry 4pxm coloured by chain, front view.
PDB entry 4pxm coloured by chain, side view.
PDB entry 4pxm coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Estrogen receptor alpha somatic mutations Y537S and D538G confer breast cancer endocrine resistance by stabilizing the activating function-2 binding conformation.
Fanning SW, Mayne CG, Dharmarajan V, Carlson KE, Martin TA, Novick SJ, Toy W, Green B, Panchamukhi S, Katzenellenbogen BS, Tajkhorshid E, Griffin PR, Shen Y, Chandarlapaty S, Katzenellenbogen JA, Greene GL
Elife 5 (2016)
PMID: 26836308

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136928 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Estrogen receptor Chains: A, B
Molecule details ›
Chains: A, B
Length: 271 amino acids
Theoretical weight: 30.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P03372 (Residues: 299-554; Coverage: 43%)
Gene names: ESR, ESR1, NR3A1
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor
Nuclear receptor coactivator 2 Chains: C, D
Molecule details ›
Chains: C, D
Length: 13 amino acids
Theoretical weight: 1.58 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q15596 (Residues: 686-698; Coverage: 1%)
Gene names: BHLHE75, NCOA2, SRC2, TIF2

Ligands and Environments

1 bound ligand:
Ligand EST 2 x EST
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P21
Unit cell:
a: 56.084Å b: 84.182Å c: 58.372Å
α: 90° β: 108.83° γ: 90°
R-values:
R R work R free
0.181 0.179 0.214
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

48 review citations

Epigenetic mechanisms in breast cancer therapy and resistance.
Garcia-Martinez et al. (2021)
47 more

5 mentions without citation

Estrogen receptor alpha somatic mutations Y537S and D538G confer breast cancer endocrine resistance by stabilizing the activating function-2 binding conformation.
Fanning et al. (2016)
4 more