Crystallization and preliminary X-ray analysis of mouse RANK and its complex with RANKL

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Jun 1;65(Pt 6):597-600. doi: 10.1107/S1744309109015735. Epub 2009 May 22.

Abstract

The interaction between the TNF-family molecule receptor activator of NF-kappaB ligand (RANKL) and its receptor RANK induces osteoclast formation, activation and survival in the process of bone remodelling. RANKL-RANK also plays critical roles in T-cell/dendritic cell communication and lymph-node formation and in a variety of pathologic conditions such as tumour-cell migration and bone metastasis. Both the ectodomain of mouse RANKL and the extracellular domain of mouse RANK have been cloned, expressed and purified. Crystals of RANK alone and of RANK in complex with RANKL have been obtained that are suitable for structure determination.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cloning, Molecular
  • Crystallization
  • Data Collection
  • Escherichia coli / genetics
  • Genetic Vectors
  • Glutathione Transferase / metabolism
  • Histidine / chemistry
  • Inclusion Bodies / metabolism
  • Mice
  • Molecular Sequence Data
  • Molecular Weight
  • Protein Folding
  • Protein Structure, Tertiary
  • RANK Ligand / chemistry
  • RANK Ligand / metabolism*
  • Receptor Activator of Nuclear Factor-kappa B / chemistry
  • Receptor Activator of Nuclear Factor-kappa B / genetics
  • Receptor Activator of Nuclear Factor-kappa B / metabolism*
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / isolation & purification
  • Recombinant Fusion Proteins / metabolism
  • Rotation
  • Solubility
  • Statistics as Topic
  • X-Ray Diffraction

Substances

  • RANK Ligand
  • Receptor Activator of Nuclear Factor-kappa B
  • Recombinant Fusion Proteins
  • Histidine
  • Glutathione Transferase