The binding of antibiotics to ERp57/GRP58

J Antibiot (Tokyo). 2008 Jun;61(6):400-2. doi: 10.1038/ja.2008.56.

Abstract

The effects of five antibiotics, previously described as ligands of protein disulfide isomerase PDI, have now been studied on the homologous protein ERp57. They bind to this protein with much higher affinity than to PDI, and some of them inhibit the reductase and the DNA-binding activities of ERp57. In view of the high affinity of vancomycin, erythromycin and streptomycin, some effects of their interaction with this protein might be expected in vivo.

MeSH terms

  • Anti-Bacterial Agents / metabolism*
  • Anti-Bacterial Agents / pharmacology
  • Binding Sites
  • DNA / metabolism
  • DNA-Binding Proteins / antagonists & inhibitors
  • Enzyme Inhibitors / metabolism*
  • Enzyme Inhibitors / pharmacology
  • Humans
  • Ligands
  • Protein Binding
  • Protein Disulfide-Isomerases / antagonists & inhibitors*
  • Protein Disulfide-Isomerases / metabolism*
  • Recombinant Proteins / antagonists & inhibitors
  • Recombinant Proteins / metabolism

Substances

  • Anti-Bacterial Agents
  • DNA-Binding Proteins
  • Enzyme Inhibitors
  • Ligands
  • Recombinant Proteins
  • DNA
  • Protein Disulfide-Isomerases
  • PDIA3 protein, human