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3dlm
From Proteopedia
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==Crystal structure of Tudor domain of human Histone-lysine N-methyltransferase SETDB1== | ==Crystal structure of Tudor domain of human Histone-lysine N-methyltransferase SETDB1== | ||
| - | <StructureSection load='3dlm' size='340' side='right' caption='[[3dlm]], [[Resolution|resolution]] 1.77Å' scene=''> | + | <StructureSection load='3dlm' size='340' side='right'caption='[[3dlm]], [[Resolution|resolution]] 1.77Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3dlm]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3dlm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DLM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DLM FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.77Å</td></tr> |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3dlm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dlm OCA], [https://pdbe.org/3dlm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dlm RCSB], [https://www.ebi.ac.uk/pdbsum/3dlm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dlm ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://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> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dl/3dlm_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dl/3dlm_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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==See Also== | ==See Also== | ||
| - | *[[Histone methyltransferase|Histone methyltransferase]] | + | *[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Amaya | + | [[Category: Amaya MF]] |
| - | [[Category: Arrowsmith | + | [[Category: Arrowsmith CH]] |
| - | [[Category: Bochkarev | + | [[Category: Bochkarev A]] |
| - | [[Category: Bountra | + | [[Category: Bountra C]] |
| - | [[Category: Dombrovski | + | [[Category: Dombrovski L]] |
| - | [[Category: Edwards | + | [[Category: Edwards AM]] |
| - | [[Category: Loppnau | + | [[Category: Loppnau P]] |
| - | [[Category: Min | + | [[Category: Min J]] |
| - | + | [[Category: Weigelt J]] | |
| - | [[Category: Weigelt | + | [[Category: Wu H]] |
| - | [[Category: Wu | + | |
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Current revision
Crystal structure of Tudor domain of human Histone-lysine N-methyltransferase SETDB1
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Categories: Homo sapiens | Large Structures | Amaya MF | Arrowsmith CH | Bochkarev A | Bountra C | Dombrovski L | Edwards AM | Loppnau P | Min J | Weigelt J | Wu H
