› 3sov

X-ray diffraction
1.27Å resolution

The structure of a beta propeller domain in complex with peptide S

Released:
DOI: 10.2210/pdb3sov/pdb
PDB entry 3sov coloured by chain, front view.
PDB entry 3sov coloured by chain, side view.
PDB entry 3sov coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Wnt antagonists bind through a short peptide to the first β-propeller domain of LRP5/6.
Bourhis E, Wang W, Tam C, Hwang J, Zhang Y, Spittler D, Huang OW, Gong Y, Estevez A, Zilberleyb I, Rouge L, Chiu C, Wu Y, Costa M, Hannoush RN, Franke Y, Cochran AG
Structure 19 1433-42 (2011)
PMID: 21944579

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131066 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Low-density lipoprotein receptor-related protein 6 Chain: A
Molecule details ›
Chain: A
Length: 318 amino acids
Theoretical weight: 35.69 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: O75581 (Residues: 20-326; Coverage: 19%)
Gene name: LRP6
Sequence domains:
Structure domains:
Sclerostin Chain: Z
Molecule details ›
Chain: Z
Length: 9 amino acids
Theoretical weight: 765 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9BQB4 (Residues: 115-121; Coverage: 4%)
Gene names: SOST, UNQ2976/PRO7455/PRO7476

Ligands and Environments

3 bound ligands:
Ligand NAG 2 x NAG
Ligand FUC 4 x FUC
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: C2
Unit cell:
a: 103.567Å b: 47.09Å c: 68.72Å
α: 90° β: 97.68° γ: 90°
R-values:
R R work R free
0.154 0.153 0.18
Expression systems:
  • Spodoptera frugiperda
  • Not provided

Quick links

Citations

31 review citations

WNT signaling in bone homeostasis and disease: from human mutations to treatments.
Baron et al. (2013)
30 more

7 mentions without citation

LRP4 third β-propeller domain mutations cause novel congenital myasthenia by compromising agrin-mediated MuSK signaling in a position-specific manner.
Ohkawara et al. (2014)
6 more