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Structure‐Based Analysis of the Effects of Camptothecin on the Activities of Human Topoisomerase I
Author(s) -
CHAMPOUX JAMES J.
Publication year - 2000
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.2000.tb07025.x
Subject(s) - topoisomerase , camptothecin , dna , chemistry , enzyme , in vitro , biochemistry , biophysics , stereochemistry , biology
A bstract : The sole target for the anticancer drug camptothecin (CPT) is the type I topoisomerase. The drug poisons the topoisomerase by slowing the religation step of the reaction, thereby trapping the enzyme in a covalent complex on the DNA. In addition, CPT has been shown to inhibit plasmid DNA relaxation in vitro . The structural bases for these two activities of CPT are explored in relation to the recently published crystal structure of the enzyme with bound DNA.