Human RecQ-Like protein 1: Difference between revisions
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The crystal structure of RECQL in complex with Mg-ADP shares the domain organization of the bacterial homologue [[1oyy | '''RecQ''']]. However, the relative position of the domains is altered: most prominently, the C-terminal winged-helix domain is completely re-oriented relative to the conserved ATPase domain. These differences may indicate that a major conformational change occurs during the active cycle of RECQ helicases. | The crystal structure of RECQL in complex with Mg-ADP shares the domain organization of the bacterial homologue [[1oyy | '''RecQ''']]. However, the relative position of the domains is altered: most prominently, the C-terminal winged-helix domain is completely re-oriented relative to the conserved ATPase domain. These differences may indicate that a major conformational change occurs during the active cycle of RECQ helicases. | ||
==Additional Resources== | |||
For additional information, see: [[DNA Replication, Repair, and Recombination]] | |||
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=== References === | === References === | ||