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Article

Effect on DNA relaxation of the single Thr718Ala mutation in human topoisomerase I: a functional and molecular dynamics study.

Nucleic acids research - 1 Jan 2005

Chillemi Giovanni, Fiorani Paola, Castelli Silvia, Bruselles Alessandro, Benedetti Piero, Desideri Alessandro

Abstract excerpt

The functional and dynamical properties of the human topoisomerase I Thr718Ala mutant have been compared to that of the wild-type enzyme using functional assays and molecular dynamics (MD) simulations. At physiological ionic strength, the cleavage and religation rates, evaluated on oligonucleotides containing the preferred topoisomerase I DNA sequence, are almost identical for the wild-type and the mutated...

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Identifiers

PMID: 15944452
DOI: 10.1093/nar/gki642
PMCID: PMC1145191

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Source receipt: pubmed, retrieved 7 Sept 2026.

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