title: Mre11-Rad50 complex crystals suggest molecular calisthenics.
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.
authors: Department of Radiation Oncology, Department of Genetics and Cancer, Erasmus University Medical Center, PO Box 2040, 3000 CA, Rotterdam, The Netherlands. c.wyman@erasmusmc.nl
authors: Claire
authors: C
authors: Wyman
authors: Joyce
authors: J
authors: Lebbink
authors: Roland
authors: R
authors: Kanaar
mesh_terms: D017766:Acid Anhydride Hydrolases; D018360:Crystallography, X-Ray; D053903:DNA Breaks, Double-Stranded; D004260:DNA Repair / Q000235:genetics; D045643:DNA Repair Enzymes / Q000737:chemistry* / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D042822:Genomic Instability; D006801:Humans; D000076228:MRE11 Homologue Protein; D008958:Models, Molecular; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary
chemical_list: D004268:DNA-Binding Proteins; C121766:MRE11 protein, human; D000076228:MRE11 Homologue Protein; D017766:Acid Anhydride Hydrolases; C112158:RAD50 protein, human; D045643:DNA Repair Enzymes