5kco
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==SETDB1 in complex with an early stage, low affinity fragment candidate modelled at reduced occupancy== | |
| - | + | <StructureSection load='5kco' size='340' side='right' caption='[[5kco]], [[Resolution|resolution]] 1.47Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5kco]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KCO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KCO FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6RO:~{N}-(4-CHLOROPHENYL)METHANESULFONAMIDE'>6RO</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr> | |
| - | [[Category: | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kch|5kch]]</td></tr> |
| - | [[Category: | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></td></tr> |
| - | [[Category: | + | <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=5kco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kco OCA], [http://pdbe.org/5kco PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kco RCSB], [http://www.ebi.ac.uk/pdbsum/5kco PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kco ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/SETB1_HUMAN SETB1_HUMAN]] Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 'Lys-9' trimethylation is coordinated with DNA methylation. Probably forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1. SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger proteins.<ref>PMID:12869583</ref> <ref>PMID:14536086</ref> <ref>PMID:15327775</ref> <ref>PMID:17952062</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Histone-lysine N-methyltransferase]] | ||
| + | [[Category: Arrowsmith, C H]] | ||
| + | [[Category: Bountra, C]] | ||
| + | [[Category: Brandao-Neto, J]] | ||
| + | [[Category: Brown, P J]] | ||
| + | [[Category: Collins, P]] | ||
| + | [[Category: Delft, F von]] | ||
[[Category: Dobrovetsky, E]] | [[Category: Dobrovetsky, E]] | ||
| + | [[Category: Douangamath, A]] | ||
| + | [[Category: Edwards, A M]] | ||
| + | [[Category: Harding, R J]] | ||
[[Category: Mader, P]] | [[Category: Mader, P]] | ||
| + | [[Category: Pearce, N]] | ||
| + | [[Category: Structural genomic]] | ||
| + | [[Category: Santhakumar, V]] | ||
| + | [[Category: Schapira, M]] | ||
[[Category: Tempel, W]] | [[Category: Tempel, W]] | ||
| - | [[Category: | + | [[Category: Walker, J R]] |
| - | [[Category: | + | [[Category: Diamond i04-1 xchem]] |
| - | [[Category: | + | [[Category: Fragment screening]] |
| - | [[Category: | + | [[Category: Pandda]] |
| - | [[Category: | + | [[Category: Sgc]] |
| - | [[Category: | + | [[Category: Transferase]] |
Revision as of 15:47, 27 July 2016
SETDB1 in complex with an early stage, low affinity fragment candidate modelled at reduced occupancy
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Categories: Histone-lysine N-methyltransferase | Arrowsmith, C H | Bountra, C | Brandao-Neto, J | Brown, P J | Collins, P | Delft, F von | Dobrovetsky, E | Douangamath, A | Edwards, A M | Harding, R J | Mader, P | Pearce, N | Structural genomic | Santhakumar, V | Schapira, M | Tempel, W | Walker, J R | Diamond i04-1 xchem | Fragment screening | Pandda | Sgc | Transferase
