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5ke3

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==Crystal structure of SETDB1 Tudor domain in complex with fragment MRT0181a==
==Crystal structure of SETDB1 Tudor domain in complex with fragment MRT0181a==
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<StructureSection load='5ke3' size='340' side='right' caption='[[5ke3]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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<StructureSection load='5ke3' size='340' side='right'caption='[[5ke3]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5ke3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KE3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KE3 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5ke3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KE3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5KE3 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6S5:(S)-N-(FURAN-2-YLMETHYL)-1-(1,2,3,4-TETRAHYDROISOQUINOLINE-3-CARBONYL)PIPERIDINE-4-CARBOXAMIDE'>6S5</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6S5:(S)-N-(FURAN-2-YLMETHYL)-1-(1,2,3,4-TETRAHYDROISOQUINOLINE-3-CARBONYL)PIPERIDINE-4-CARBOXAMIDE'>6S5</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
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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=5ke3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ke3 OCA], [http://pdbe.org/5ke3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ke3 RCSB], [http://www.ebi.ac.uk/pdbsum/5ke3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ke3 ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SETDB1, KIAA0067, KMT1E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ke3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ke3 OCA], [http://pdbe.org/5ke3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ke3 RCSB], [http://www.ebi.ac.uk/pdbsum/5ke3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ke3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>
[[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>
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==See Also==
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*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith, C H]]
[[Category: Bountra, C]]
[[Category: Bountra, C]]

Revision as of 15:23, 8 July 2020

Crystal structure of SETDB1 Tudor domain in complex with fragment MRT0181a

PDB ID 5ke3

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