› 1jdp

X-ray diffraction
2Å resolution

Crystal Structure of Hormone/Receptor Complex

Released:
DOI: 10.2210/pdb1jdp/pdb
PDB entry 1jdp coloured by chain, front view.
PDB entry 1jdp coloured by chain, side view.
PDB entry 1jdp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Allosteric activation of a spring-loaded natriuretic peptide receptor dimer by hormone.
Martick MM, Garcia KC
Science 293 1657-62 (2001)
PMID: 11533490

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148040 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Atrial natriuretic peptide receptor 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 441 amino acids
Theoretical weight: 49.54 KDa
Source organism: Homo sapiens
Expression system: Drosophila
UniProt:
  • Canonical: P17342 (Residues: 44-485; Coverage: 86%)
Gene names: ANPRC, C5orf23, NPR3, NPRC
Sequence domains: Receptor family ligand binding region
Structure domains: Rossmann fold
CNP-22 Chain: H
Molecule details ›
Chain: H
Length: 22 amino acids
Theoretical weight: 2.2 KDa
Source organism: Homo sapiens
Expression system: Drosophila
UniProt:
  • Canonical: P23582 (Residues: 105-126; Coverage: 21%)
Gene names: CNP2, NPPC
Sequence domains: Atrial natriuretic peptide

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
2 bound ligands:
Ligand NAG 3 x NAG
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P212121
Unit cell:
a: 56.8Å b: 136.455Å c: 137.591Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.227 0.248
Expression system: Drosophila

Quick links

Citations

41 review citations

Coupling of folding and binding for unstructured proteins.
Dyson et al. (2002)
40 more

9 mentions without citation

Mutations in the transmembrane natriuretic peptide receptor NPR-B impair skeletal growth and cause acromesomelic dysplasia, type Maroteaux.
Bartels et al. (2004)
8 more