› 1ya3

X-ray diffraction
2.34Å resolution

Crystal structure of the human mineralocorticoid receptor ligand-binding domain bound to progesterone and harboring the S810L mutation responsible for a severe form of hypertension

Released:
DOI: 10.2210/pdb1ya3/pdb
PDB entry 1ya3 coloured by chain, front view.
PDB entry 1ya3 coloured by chain, side view.
PDB entry 1ya3 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of a mutant mineralocorticoid receptor responsible for hypertension.
Fagart J, Huyet J, Pinon GM, Rochel M, Mayer C, Rafestin-Oblin ME
Nat Struct Mol Biol 12 554-5 (2005)
PMID: 15908963

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140040 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mineralocorticoid receptor Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 255 amino acids
Theoretical weight: 29.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08235 (Residues: 731-984; Coverage: 26%)
Gene names: MCR, MLR, NR3C2
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor

Ligands and Environments

1 bound ligand:
Ligand STR 3 x STR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P31
Unit cell:
a: 120.724Å b: 120.724Å c: 42.508Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.252 0.237 0.284
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Structural overview of the nuclear receptor superfamily: insights into physiology and therapeutics.
Huang et al. (2010)
15 more

2 mentions without citation

Structural protein-ligand interaction fingerprints (SPLIF) for structure-based virtual screening: method and benchmark study.
Da et al. (2014)
1 more