Reciprocal “flipping” underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase

Both 8oxo-guanine and formamidopyrimidines are major products of oxidative DNA damage that can result in the fixation of transversion mutations following replication if left unrepaired. These lesions are targeted by the N-DNA glycosylase hOgg1, which catalyses excision of the aberrant base followed...

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Veröffentlicht in:	Journal of molecular biology 2002-03, Vol.317 (2), p.171-177
Hauptverfasser:	Bjørås, Magnar, Seeberg, Erling, Luna, Luisa, Pearl, Laurence H, Barrett, Tracey E
Format:	Artikel
Sprache:	eng
Schlagworte:	8-oxoguanine-DNA glycosylase 8oxo-guanine DNA-glycosylase Binding Sites Catalytic Domain crystal structure Crystallography, X-Ray DNA - metabolism DNA-Formamidopyrimidine Glycosylase Enzyme Activation Guanine - analogs & derivatives Guanine - metabolism hOgg1 protein Humans Hydrogen Bonding Models, Molecular Mutagenesis, Site-Directed N-Glycosyl Hydrolases - chemistry N-Glycosyl Hydrolases - genetics N-Glycosyl Hydrolases - metabolism nucleophilic attack Protein Conformation reciprocal flipping specificity pocket
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