Probing the structural basis of RecQ helicase function.
|Abstract||RecQ helicases are a ubiquitous family of DNA unwinding enzymes required to preserve genome integrity, thus preventing premature aging and cancer formation. The five human representatives of this family play non-redundant roles in the suppression of genome instability using a combination of enzymatic activities that specifically characterize each member of the family. These enzymes are in fact not only able to catalyze the transient opening of DN ... [truncated at 450 characters in length]|
|Author||Vindigni, Alessandro; Marino, Francesca; Gileadi, Opher;|
|Subject||DNA Repair DNA Replication DNA, Cruciform Genomic Instability Humans Protein Structure, Tertiary RecQ Helicases chemistry metabolism chemistry metabolism|
A prominent beta-hairpin structure in the winged-helix domain of RECQ1 is required for DNA unwinding and oligomer formation.
|Abstract||RecQ helicases have attracted considerable interest in recent years due to their role in the suppression of genome instability and human diseases. These atypical helicases exert their function by resolving a number of highly specific DNA structures. The crystal structure of a truncated catalytic core of the human RECQ1 helicase (RECQ1(49-616)) shows a prominent β-hairpin, with an aromatic residue (Y564) at the tip, located in the C-terminal winge ... [truncated at 450 characters in length]|
|Author||Lucic, Bojana; Zhang, Ying; King, Oliver; et al|
|Subject||DNA DNA, Cruciform Dimerization Humans Protein Multimerization Protein Structure, Secondary Protein Structure, Tertiary RecQ Helicases metabolism chemistry metabolism|