Sandbox GGC15
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==DNA TOPOISOMERASE I== | ==DNA TOPOISOMERASE I== | ||
<StructureSection load='1A36' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1A36' size='340' side='right' caption='Caption for this structure' scene=''> | ||
| - | + | Eukaryotic DNA topoisomerase I (topo I) is a protein that reduces the strain from the supercoils that are caused during transcription and translation<ref>DOI 10.1073/pnas.242259599</ref>. There are two types of topoisomerases. Type 1 topoisomerases are monomeric and break one strand of DNA<ref>PMID:9488644</ref>. Type 2 topoisomerases are dimeric, meaning that they made up of two units and break both strands of the DNA helix. They are able to pass another part of the duplex through the cut, and close the cut using ATP<ref>PMID:9488644</ref>. | |
| - | + | ||
| - | + | ||
== Function == | == Function == | ||
| - | + | ||
== Disease == | == Disease == | ||
Revision as of 20:10, 27 April 2021
DNA TOPOISOMERASE I
| |||||||||||
References
- ↑ Staker BL, Hjerrild K, Feese MD, Behnke CA, Burgin AB Jr, Stewart L. The mechanism of topoisomerase I poisoning by a camptothecin analog. Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15387-92. Epub 2002 Nov 8. PMID:12426403 doi:10.1073/pnas.242259599
- ↑ Redinbo MR, Stewart L, Kuhn P, Champoux JJ, Hol WG. Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA. Science. 1998 Mar 6;279(5356):1504-13. PMID:9488644
- ↑ Redinbo MR, Stewart L, Kuhn P, Champoux JJ, Hol WG. Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA. Science. 1998 Mar 6;279(5356):1504-13. PMID:9488644
