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{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/4103454","sourcedb":"PMC","sourceid":"4103454","source_url":"https://www.ncbi.nlm.nih.gov/pmc/4103454","text":"The Fanconi anemia pathway is responsible for clearing DNA interstrand crosslinks that block DNA replication and transcription leading to genome instability. Here, Pennell et al. characterize the Fanconi-anemia-associated nuclease FAN1, comparing the structure and activity of its catalytic VRR-Nuc domain with prokaryotic examples. FAN1 is monomeric with 5′ flap specificity, whereas prokaryotic VRR-Nuc domains are dimeric Holliday-junction-resolving enzymes. FAN1 is proposed to contain a conserved helical insertion blocking dimer formation and consequently restricting substrate specificity.\n","tracks":[]}