1a31
From Proteopedia
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HUMAN RECONSTITUTED DNA TOPOISOMERASE I IN COVALENT COMPLEX WITH A 22 BASE PAIR DNA DUPLEX
Contents |
Overview
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.
Disease
Known disease associated with this structure: DNA topoisomerase I, camptothecin-resistant OMIM:[126420]
About this Structure
1A31 is a Single protein structure of sequence from Homo sapiens. The following page contains interesting information on the relation of 1A31 with [Topoisomerases]. Active as DNA topoisomerase, with EC number 5.99.1.2 Full crystallographic information is available from OCA.
Reference
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
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