3qx3

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qx3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qx3 RCSB], [http://www.ebi.ac.uk/pdbsum/3qx3 PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qx3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qx3 RCSB], [http://www.ebi.ac.uk/pdbsum/3qx3 PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/TOP2B_HUMAN TOP2B_HUMAN]] Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. Indirectly involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene.<ref>PMID:10684600</ref> <ref>PMID:12837248</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 13:31, 25 December 2014

Human topoisomerase IIbeta in complex with DNA and etoposide

3qx3, resolution 2.16Å

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