title: SUMO modification: wrestling with protein conformation.
abstract: SUMO modification of human thymine-DNA glycosylase facilitates the processing of base excision repair substrates by an unusual mechanism: while leaving the catalytic center unaffected, it induces product release by eliciting a conformational change in the enzyme.
authors.affiliation: Cancer Research UK, Clare Hall Laboratories, South Mimms, UK. helle.ulrich@cancer.org.uk <helle.ulrich@cancer.org.uk>
authors.forename: Helle D
authors.initials: HD
authors.lastname: Ulrich
mesh_terms: D002384:Catalysis; D004260:DNA Repair / Q000235:genetics / Q000502:physiology*; D006801:Humans; D008954:Models, Biological; D011485:Protein Binding; D011487:Protein Conformation; D025842:SUMO-1 Protein / Q000378:metabolism*; D044502:Thymine DNA Glycosylase / Q000378:metabolism*
chemical_list: D025842:SUMO-1 Protein; D044502:Thymine DNA Glycosylase