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Article

Single mutation in the linker domain confers protein flexibility and camptothecin resistance to human topoisomerase I.

The Journal of biological chemistry - 31 Oct 2003

Fiorani Paola, Bruselles Alessandro, Falconi Mattia, Chillemi Giovanni, Desideri Alessandro, Benedetti Piero

Abstract excerpt

DNA topoisomerase I relaxes supercoiled DNA by the formation of a covalent intermediate in which the active-site tyrosine is transiently bound to the cleaved DNA strand. The antineoplastic agent camptothecin specifically targets DNA topoisomerase I, and several mutations have been isolated that render the enzyme camptothecin-resistant. The catalytic and structural dynamical properties of a human DNA topoisomerase...

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Identifiers

PMID: 12904303
DOI: 10.1074/jbc.M303899200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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