Sandbox Reserved 390: Difference between revisions
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The interplay between the <scene name='Sandbox_Reserved_390/Top/6'>protein</scene>, the <scene name='Sandbox_Reserved_390/Top/5'>DNA</scene>, and the drug explains the structure-activity relations of etoposide derivatives and the molecular basis of drug-resistant mutations. | The interplay between the <scene name='Sandbox_Reserved_390/Top/6'>protein</scene>, the <scene name='Sandbox_Reserved_390/Top/5'>DNA</scene>, and the drug explains the structure-activity relations of etoposide derivatives and the molecular basis of drug-resistant mutations. | ||
Also, at the <scene name='Sandbox_Reserved_390/Top/1'>active site</scene> we can see | Also, at the <scene name='Sandbox_Reserved_390/Top/1'>active site</scene> we can see the <scene name='Sandbox_Reserved_390/Top/7'>ligand</scene>, and both <scene name='Sandbox_Reserved_390/Top/3'>alpha helices</scene>, and <scene name='Sandbox_Reserved_390/Top/2'>beta sheets</scene> at the <scene name='Sandbox_Reserved_390/Top/4'>secondary structures</scene>. | ||
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==References== | ==References== | ||
<references /> | <references /> | ||
Revision as of 17:28, 19 September 2012
Human topoisomerase IIbeta in complex with DNA and etoposide
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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[1].
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.
Also, at the active site we can see the ligand, and both alpha helices, and beta sheets at the secondary structures.
References
- ↑ 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
