5emx
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the S. cerevisiae Rtf1 histone modification domain mutant R124A R126A R128A== | |
| - | + | <StructureSection load='5emx' size='340' side='right' caption='[[5emx]], [[Resolution|resolution]] 1.40Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5emx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EMX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EMX FirstGlance]. <br> | |
| - | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5e8b|5e8b]]</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=5emx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5emx OCA], [http://pdbe.org/5emx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5emx RCSB], [http://www.ebi.ac.uk/pdbsum/5emx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5emx ProSAT]</span></td></tr> |
| - | [[ | + | </table> |
| - | [[ | + | == Function == |
| + | [[http://www.uniprot.org/uniprot/RTF1_YEAST RTF1_YEAST]] The PAF1 complex is a multifunctional complex. Involved in transcription initiation via genetic interactions with TATA-binding proteins. Involved in elongation. It regulates 3'-end formation of snR47 by modulating the recruitment or stable association of NRD1 and NAB3 with RNA polymerase II. Also has a role in transcription-coupled histone modification. Required for activation of RAD6 ubiquitin conjugate and the BRE1 ubiquitin ligase which ubiquitinate 'Lys-126' histone H2B. Activates the SET1 histone methyltransferase complex for methylation of 'Lys-4' of histone H3 and for methylation of 'Lys-73' of histone H3 by DOT1 and 'Lys-36' of histone H3 by SET2. Important for TATA site selection by TBP. Directly or indirectly regulates the DNA-binding properties of SPT15, the TATA box-binding protein, and the relative activities of different TATA elements.<ref>PMID:15643076</ref> <ref>PMID:16246725</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Heroux, A]] | [[Category: Heroux, A]] | ||
| + | [[Category: VanDemark, A P]] | ||
| + | [[Category: Wier, A D]] | ||
| + | [[Category: Chromatin]] | ||
| + | [[Category: Paf1]] | ||
| + | [[Category: Rtf1]] | ||
| + | [[Category: Transcription]] | ||
Revision as of 18:40, 26 October 2016
Crystal structure of the S. cerevisiae Rtf1 histone modification domain mutant R124A R126A R128A
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Categories: Heroux, A | VanDemark, A P | Wier, A D | Chromatin | Paf1 | Rtf1 | Transcription
