› 1upv

X-ray diffraction
2.1Å resolution

Crystal structure of the human Liver X receptor beta ligand binding domain in complex with a synthetic agonist

Released:
DOI: 10.2210/pdb1upv/pdb
PDB entry 1upv coloured by chain, front view.
PDB entry 1upv coloured by chain, side view.
PDB entry 1upv coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the human liver X receptor beta ligand-binding domain in complex with a synthetic agonist.
Hoerer S, Schmid A, Heckel A, Budzinski RM, Nar H
J Mol Biol 334 853-61 (2003)
PMID: 14643652

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157159 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Oxysterols receptor LXR-beta Chain: A
Molecule details ›
Chain: A
Length: 257 amino acids
Theoretical weight: 29.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P55055 (Residues: 203-460; Coverage: 56%)
Gene names: LXRB, NER, NR1H2, UNR
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor

Ligands and Environments

1 bound ligand:
Ligand 444 1 x 444
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: C2
Unit cell:
a: 141.8Å b: 43.2Å c: 51.8Å
α: 90° β: 105.8° γ: 90°
R-values:
R R work R free
0.215 0.215 0.274
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

International Union of Pharmacology. LXII. The NR1H and NR1I receptors: constitutive androstane receptor, pregnene X receptor, farnesoid X receptor alpha, farnesoid X receptor beta, liver X receptor alpha, liver X receptor beta, and vitamin D receptor.
Moore et al. (2006)
4 more

8 mentions without citation

Drug discovery using chemical systems biology: identification of the protein-ligand binding network to explain the side effects of CETP inhibitors.
Xie et al. (2009)
7 more