3dlm

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<StructureSection load='3dlm' size='340' side='right'caption='[[3dlm]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
<StructureSection load='3dlm' size='340' side='right'caption='[[3dlm]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3dlm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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>
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<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>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SETDB1, KIAA0067, KMT1E ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.77&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></td></tr>
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<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'>[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>
</table>
</table>
== Function ==
== Function ==
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[[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>
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[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]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Histone-lysine N-methyltransferase]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Amaya, M F]]
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[[Category: Amaya MF]]
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[[Category: Arrowsmith, C H]]
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[[Category: Arrowsmith CH]]
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[[Category: Bochkarev, A]]
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[[Category: Bochkarev A]]
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[[Category: Bountra, C]]
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[[Category: Bountra C]]
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[[Category: Dombrovski, L]]
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[[Category: Dombrovski L]]
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[[Category: Edwards, A M]]
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[[Category: Edwards AM]]
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[[Category: Loppnau, P]]
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[[Category: Loppnau P]]
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[[Category: Min, J]]
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[[Category: Min J]]
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[[Category: Structural genomic]]
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[[Category: Weigelt J]]
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[[Category: Weigelt, J]]
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[[Category: Wu H]]
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[[Category: Wu, H]]
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[[Category: Alternative splicing]]
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[[Category: Chromatin regulator]]
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[[Category: Chromosomal protein]]
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[[Category: Coiled coil]]
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[[Category: Histone-lysine n-methyltransferase]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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[[Category: Polymorphism]]
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[[Category: Repressor]]
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[[Category: S-adenosyl-l-methionine]]
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[[Category: Setdb1_human]]
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[[Category: Sgc]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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[[Category: Transferase]]
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Current revision

Crystal structure of Tudor domain of human Histone-lysine N-methyltransferase SETDB1

PDB ID 3dlm

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