Sandbox Reserved 390: Difference between revisions

From Proteopedia
Jump to navigationJump to search
No edit summary
No edit summary
Line 1: Line 1:
=== '''Human topoisomerase IIbeta in complex with DNA and etoposide''' ===
=== '''Human topoisomerase IIbeta in complex with DNA and etoposide''' ===
<Structure load='3qx3' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /><!-- PLEASE DO NOT DELETE THIS TEMPLATE -->
<Structure load='3qx3' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /><!-- PLEASE DO NOT DELETE THIS TEMPLATE -->
<ref>PMID: 21778401</ref>
 
Crystal structure of a large fragment of human type II topoisomerases (TOP2) complexed to DNA and to the anticancer drug etoposide to reveal structural details of drug-induced stabilization of a cleavage complex. The interplay between the protein, the DNA, and the drug explains the structure-activity relations of etoposide derivatives and the molecular basis of drug-resistant mutations. <ref>PMID: 21778401</ref>
<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->


==References==
==References==
<references />
<references />

Revision as of 02:39, 19 September 2012

Human topoisomerase IIbeta in complex with DNA and etoposide

Insert caption here

Drag the structure with the mouse to rotate

Crystal structure of a large fragment of human type II topoisomerases (TOP2) complexed to DNA and to the anticancer drug etoposide to reveal structural details of drug-induced stabilization of a cleavage complex. The interplay between the protein, the DNA, and the drug explains the structure-activity relations of etoposide derivatives and the molecular basis of drug-resistant mutations. [1]

References

  1. ↑ Wu CC, Li TK, Farh L, Lin LY, Lin TS, Yu YJ, Yen TJ, Chiang CW, Chan NL. Structural basis of type II topoisomerase inhibition by the anticancer drug etoposide. Science. 2011 Jul 22;333(6041):459-62. PMID:21778401 doi:10.1126/science.1204117