4e47: Difference between revisions

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==SET7/9 in complex with inhibitor (R)-(3-(3-cyanophenyl)-1-oxo-1-(pyrrolidin-1-yl)propan-2-yl)-1,2,3,4-tetrahydroisoquinoline-6- sulfonamide and S-adenosylmethionine==
==SET7/9 in complex with inhibitor (R)-(3-(3-cyanophenyl)-1-oxo-1-(pyrrolidin-1-yl)propan-2-yl)-1,2,3,4-tetrahydroisoquinoline-6- sulfonamide and S-adenosylmethionine==
<StructureSection load='4e47' size='340' side='right' caption='[[4e47]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='4e47' size='340' side='right'caption='[[4e47]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4e47]] is a 4 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=4E47 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E47 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4e47]] is a 4 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=4E47 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E47 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0N6:(R)-(3-(3-CYANOPHENYL)-1-OXO-1-(PYRROLIDIN-1-YL)PROPAN-2-YL)-1,2,3,4-TETRAHYDROISOQUINOLINE-6-SULFONAMIDE'>0N6</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0N6:(R)-(3-(3-CYANOPHENYL)-1-OXO-1-(PYRROLIDIN-1-YL)PROPAN-2-YL)-1,2,3,4-TETRAHYDROISOQUINOLINE-6-SULFONAMIDE'>0N6</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SETD7, KIAA1717, KMT7, SET7, SET9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4e47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e47 OCA], [https://pdbe.org/4e47 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e47 RCSB], [https://www.ebi.ac.uk/pdbsum/4e47 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e47 ProSAT]</span></td></tr>
<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>
<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=4e47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e47 OCA], [http://pdbe.org/4e47 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4e47 RCSB], [http://www.ebi.ac.uk/pdbsum/4e47 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4e47 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SETD7_HUMAN SETD7_HUMAN]] Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation.<ref>PMID:12588998</ref> <ref>PMID:15099517</ref> <ref>PMID:16141209</ref> <ref>PMID:17108971</ref> <ref>PMID:12540855</ref> <ref>PMID:15525938</ref>
[[https://www.uniprot.org/uniprot/SETD7_HUMAN SETD7_HUMAN]] Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation.<ref>PMID:12588998</ref> <ref>PMID:15099517</ref> <ref>PMID:16141209</ref> <ref>PMID:17108971</ref> <ref>PMID:12540855</ref> <ref>PMID:15525938</ref>  
 
==See Also==
*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Histone-lysine N-methyltransferase]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith CH]]
[[Category: Barsyte, D]]
[[Category: Barsyte D]]
[[Category: Bountra, C]]
[[Category: Bountra C]]
[[Category: Brown, P J]]
[[Category: Brown PJ]]
[[Category: Bunnage, M]]
[[Category: Bunnage M]]
[[Category: Cook, A]]
[[Category: Cook A]]
[[Category: Dong, A]]
[[Category: Dong A]]
[[Category: Edwards, A M]]
[[Category: Edwards AM]]
[[Category: Fish, P]]
[[Category: Fish P]]
[[Category: Ouyang, H]]
[[Category: Ouyang H]]
[[Category: Owen, D]]
[[Category: Owen D]]
[[Category: Structural genomic]]
[[Category: Tatlock J]]
[[Category: Tatlock, J]]
[[Category: Vedadi M]]
[[Category: Vedadi, M]]
[[Category: Walker JR]]
[[Category: Walker, J R]]
[[Category: Weigelt J]]
[[Category: Weigelt, J]]
[[Category: Chromatin regulator]]
[[Category: Chromosomal protein]]
[[Category: Inhibitor]]
[[Category: Methyltransferase]]
[[Category: Nucleus]]
[[Category: S-adenosylmethionine]]
[[Category: Set domain]]
[[Category: Sgc]]
[[Category: Ternary complex]]
[[Category: Transcription]]
[[Category: Transcription regulation]]
[[Category: Transferase]]
[[Category: Transferase-transferase inhibitor complex]]

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