Sandbox Reserved 390: Difference between revisions

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__TOC__

==INTRODUCTION ==

The research team described the structural basis by which an anticancer drug etoposide kills cancer cells by interacting with its cellular targets human DNA topoisomerase type II<ref>PMID: 21778401</ref>. In the close-up representation of the <scene name='Sandbox_Reserved_390/Top/21'>etoposide-binding site(s),</scene> cartoon-and-stick representation shows the insertion of two etoposide molecules into two cleavage sites [etoposide surrounded by orange mesh that represent active site (etoposide in red & grey representation), the DNA chain is in red and blue, and the magnesium is in green].

The research team described the structural basis by which an anticancer drug etoposide kills cancer cells by interacting with its cellular targets human DNA topoisomerase type II<ref>PMID: 21778401</ref>. In the close-up representation of the <scene name='Sandbox_Reserved_390/Top/21'>etoposide-binding site(s),</scene> cartoon-and-stick representation shows the insertion of two etoposide molecules into two cleavage sites [etoposide surrounded by orange mesh that represent active site (etoposide in red & grey representation), the DNA chain is in red and blue, and the magnesium is in green]. The neighboring magnesium’s are believed to be use at both the ATP-binding domain and in the cleavage core. In the nucleotide-binding pocket magnesium has been shown to contact all of the phosphate groups and it’s possible that the change in magnesium can be linked to a diminishing in the nucleotide-binding pocket.

==ENZYME==

Type II topoisomerases (TOP2s) are abundant enzymes that play an essential role in <scene name='Sandbox_Reserved_390/Top/5'>DNA</scene> replication and transcription and are important targets for cancer chemotherapeutic drugs. These enzymes briefly cleave a pair of opposing phosphodiester bonds four base pairs apart, generating a TOP2-DNA cleavage complex.

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@@ Line 6: / Line 6: @@
 __TOC__
 ==INTRODUCTION ==
-The research team described the structural basis by which an anticancer drug etoposide kills cancer cells by interacting with its cellular targets human DNA topoisomerase type II<ref>PMID: 21778401</ref>. In the close-up representation of the <scene name='Sandbox_Reserved_390/Top/21'>etoposide-binding site(s),</scene> cartoon-and-stick representation shows the insertion of two etoposide molecules into two cleavage sites [etoposide surrounded by orange mesh that represent active site (etoposide in red & grey representation), the DNA chain is in red and blue, and the magnesium is in green].
+The research team described the structural basis by which an anticancer drug etoposide kills cancer cells by interacting with its cellular targets human DNA topoisomerase type II<ref>PMID: 21778401</ref>. In the close-up representation of the <scene name='Sandbox_Reserved_390/Top/21'>etoposide-binding site(s),</scene> cartoon-and-stick representation shows the insertion of two etoposide molecules into two cleavage sites [etoposide surrounded by orange mesh that represent active site (etoposide in red & grey representation), the DNA chain is in red and blue, and the magnesium is in green]. The neighboring magnesium’s are believed to be use at both the ATP-binding domain and in the cleavage core. In the nucleotide-binding pocket magnesium has been shown to contact all of the phosphate groups and it’s possible that the change in magnesium can be linked to a diminishing in the nucleotide-binding pocket.
 ==ENZYME==
 Type II topoisomerases (TOP2s) are abundant enzymes that play an essential role in <scene name='Sandbox_Reserved_390/Top/5'>DNA</scene> replication and transcription and are important targets for cancer chemotherapeutic drugs. These enzymes briefly cleave a pair of opposing phosphodiester bonds four base pairs apart, generating a TOP2-DNA cleavage complex.