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Article

Mutation of Gly721 alters DNA topoisomerase I active site architecture and sensitivity to camptothecin.

The Journal of biological chemistry - 8 Feb 2008

van der Merwe Marié, Bjornsti Mary-Ann

Abstract excerpt

DNA topoisomerase I (Top1p) catalyzes the relaxation of supercoiled DNA via a concerted mechanism of DNA strand cleavage and religation. Top1p is the cellular target of the anti-cancer drug camptothecin (CPT), which reversibly stabilizes a covalent enzyme-DNA intermediate. Top1p clamps around duplex DNA, wherein the core and C-terminal domains are connected by extended alpha-helices (linker domain), which...

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Identifiers

PMID: 18056711
DOI: 10.1074/jbc.M705781200
PMCID: PMC4995888

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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