1a35: Difference between revisions
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'''HUMAN TOPOISOMERASE I/DNA COMPLEX''' | '''HUMAN TOPOISOMERASE I/DNA COMPLEX''' | ||
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[[Category: Redinbo, M R.]] | [[Category: Redinbo, M R.]] | ||
[[Category: Stewart, L.]] | [[Category: Stewart, L.]] | ||
[[Category: | [[Category: Dna]] | ||
[[Category: | [[Category: Topoisomerase i]] | ||
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Revision as of 09:44, 2 May 2008
HUMAN TOPOISOMERASE I/DNA COMPLEX
OverviewOverview
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.
About this StructureAbout this Structure
1A35 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA., Redinbo MR, Stewart L, Kuhn P, Champoux JJ, Hol WG, Science. 1998 Mar 6;279(5356):1504-13. PMID:9488644 Page seeded by OCA on Fri May 2 09:44:25 2008