› 3c4m

X-ray diffraction
1.95Å resolution

Structure of human parathyroid hormone in complex with the extracellular domain of its G-protein-coupled receptor (PTH1R)

Released:
DOI: 10.2210/pdb3c4m/pdb
PDB entry 3c4m coloured by chain, front view.
PDB entry 3c4m coloured by chain, side view.
PDB entry 3c4m coloured by chain, top view.
Source organisms:
Primary publication:
Molecular recognition of parathyroid hormone by its G protein-coupled receptor.
Pioszak AA, Xu HE
Proc Natl Acad Sci U S A 105 5034-9 (2008)
PMID: 18375760

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-134142 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Maltose/maltodextrin-binding periplasmic protein; Parathyroid hormone/parathyroid hormone-related peptide receptor Chains: A, B
Molecule details ›
Chains: A, B
Length: 539 amino acids
Theoretical weight: 60.3 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEX9 (Residues: 25-392; Coverage: 99%)
  • Canonical: Q03431 (Residues: 29-187; Coverage: 28%)
Gene names: JW3994, PTH1R, PTHR, PTHR1, b4034, malE
Sequence domains:
Structure domains:
Parathyroid hormone Chains: C, D
Molecule details ›
Chains: C, D
Length: 21 amino acids
Theoretical weight: 2.55 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P01270 (Residues: 46-65; Coverage: 22%)
Gene name: PTH

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P21
Unit cell:
a: 62.919Å b: 116.791Å c: 78.416Å
α: 90° β: 108.8° γ: 90°
R-values:
R R work R free
0.188 0.186 0.227
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

28 review citations

Seven transmembrane receptors as shapeshifting proteins: the impact of allosteric modulation and functional selectivity on new drug discovery.
Kenakin et al. (2010)
27 more

29 mentions without citation

Receptor Activity-Modifying Proteins (RAMPs): New Insights and Roles.
Hay et al. (2016)
28 more