Mre11-Rad50 complex crystals suggest molecular calisthenics

DNA Repair (Amst). 2011 Oct 10;10(10):1066-70. doi: 10.1016/j.dnarep.2011.07.008. Epub 2011 Sep 4.

Abstract

Recently published crystal structures of different Mre11 and Rad50 complexes show the arrangement of these proteins and imply dramatic ligand-induced rearrangements with important functional consequences.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallography, X-Ray
  • DNA Breaks, Double-Stranded
  • DNA Repair / genetics
  • DNA Repair Enzymes / chemistry*
  • DNA Repair Enzymes / metabolism
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / metabolism
  • Genomic Instability
  • Humans
  • MRE11 Homologue Protein
  • Models, Molecular
  • Protein Multimerization
  • Protein Structure, Tertiary

Substances

  • DNA-Binding Proteins
  • MRE11 protein, human
  • MRE11 Homologue Protein
  • Rad50 protein, human
  • DNA Repair Enzymes