1a35

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{{STRUCTURE_1a35| PDB=1a35 | SCENE= }}
{{STRUCTURE_1a35| PDB=1a35 | SCENE= }}
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'''HUMAN TOPOISOMERASE I/DNA COMPLEX'''
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===HUMAN TOPOISOMERASE I/DNA COMPLEX===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9488644 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9488644}}
==About this Structure==
==About this Structure==
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[[Category: Dna]]
[[Category: Dna]]
[[Category: Topoisomerase i]]
[[Category: Topoisomerase i]]
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Revision as of 12:54, 30 June 2008

Image:1a35.png

Template:STRUCTURE 1a35

HUMAN TOPOISOMERASE I/DNA COMPLEX

Template:ABSTRACT PUBMED 9488644

About this Structure

1A35 is a Single protein structure of sequence from Homo sapiens. 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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