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Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA | M R Redinbo
; L Stewart
; P Kuhn
; J J Champoux
; W G Hol
; | Date: |
6 Mar 1998 | Journal: | Science, 279 (5356), 1504-13 | Abstract: | Topoisomerases I promote the relaxation of DNA superhelical tension by introducing a transient single-stranded break in duplex DNA and are vital for the processes of replication, transcription, and recombination. The crystal structures at 2.1 and 2.5 angstrom resolution of reconstituted human topoisomerase I comprising the core and carboxyl-terminal domains in covalent and noncovalent complexes with 22-base pair DNA duplexes reveal an enzyme that "clamps" around essentially B-form DNA. The core domain and the first eight residues of the carboxyl-terminal domain of the enzyme, including the active-site nucleophile tyrosine-723, share significant structural similarity with the bacteriophage family of DNA integrases. A binding mode for the anticancer drug camptothecin is proposed on the basis of chemical and biochemical information combined with these three-dimensional structures of topoisomerase I-DNA complexes. | Source: | PubMed, pmid9488644 | Services: | Forum | Review | Favorites |
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