3vp8

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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=3vp8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vp8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vp8 RCSB], [http://www.ebi.ac.uk/pdbsum/3vp8 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=3vp8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vp8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vp8 RCSB], [http://www.ebi.ac.uk/pdbsum/3vp8 PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/TUP1_YEAST TUP1_YEAST]] Acts as component of the CYC8-TUP1 corepressor complex which is involved in the repression of many genes in a wide variety of physiological processes including heme-regulated and catabolite repressed genes. May also be involved in the derepression of at least some target genes. The complex is recruited to target genes by interaction with DNA-bound transcriptional repressors, like MATALPHA2, MIG1, RFX1 and SKO1. The complex recruits histone deacetylases to produce a repressive chromatin structure, interacts with hypoacetylated N-terminal tails of histones H3 and H4 that have been programmed for repression by the action of histone deacetylases and interferes directly with the transcriptional machinery by associating with the RNA polymerase II mediator complex.<ref>PMID:2247069</ref> <ref>PMID:11069890</ref> <ref>PMID:10722672</ref> <ref>PMID:11230135</ref> <ref>PMID:11172717</ref> <ref>PMID:11784848</ref> <ref>PMID:14665463</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 05:55, 25 December 2014

Crystal structure of the N-terminal domain of the yeast general corepressor Tup1p

3vp8, resolution 1.91Å

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