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3vv0
From Proteopedia
(Difference between revisions)
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<StructureSection load='3vv0' size='340' side='right' caption='[[3vv0]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3vv0' size='340' side='right' caption='[[3vv0]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3vv0]] 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=3VV0 OCA]. <br> | + | <table><tr><td colspan='2'>[[3vv0]] 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=3VV0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VV0 FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=KH3:5-{[(3S)-3-AMINO-3-CARBOXYPROPYL][2-(HEXYLAMINO)ETHYL]AMINO}-5-DEOXYADENOSINE'>KH3</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=KH3:5-{[(3S)-3-AMINO-3-CARBOXYPROPYL][2-(HEXYLAMINO)ETHYL]AMINO}-5-DEOXYADENOSINE'>KH3</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vuz|3vuz]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vuz|3vuz]]</td></tr> |
| - | <tr><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='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><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ | + | <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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vv0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vv0 RCSB], [http://www.ebi.ac.uk/pdbsum/3vv0 PDBsum]</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=3vv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vv0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vv0 RCSB], [http://www.ebi.ac.uk/pdbsum/3vv0 PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == 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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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Structures of histone methyltransferase SET7/9 in complexes with adenosylmethionine derivatives.,Niwa H, Handa N, Tomabechi Y, Honda K, Toyama M, Ohsawa N, Shirouzu M, Kagechika H, Hirano T, Umehara T, Yokoyama S Acta Crystallogr D Biol Crystallogr. 2013 Apr;69(Pt 4):595-602. doi:, 10.1107/S0907444912052092. Epub 2013 Mar 14. PMID:23519668<ref>PMID:23519668</ref> | Structures of histone methyltransferase SET7/9 in complexes with adenosylmethionine derivatives.,Niwa H, Handa N, Tomabechi Y, Honda K, Toyama M, Ohsawa N, Shirouzu M, Kagechika H, Hirano T, Umehara T, Yokoyama S Acta Crystallogr D Biol Crystallogr. 2013 Apr;69(Pt 4):595-602. doi:, 10.1107/S0907444912052092. Epub 2013 Mar 14. PMID:23519668<ref>PMID:23519668</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Histone methyltransferase|Histone methyltransferase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 23: | Line 28: | ||
[[Category: Histone-lysine N-methyltransferase]] | [[Category: Histone-lysine N-methyltransferase]] | ||
[[Category: Human]] | [[Category: Human]] | ||
| - | [[Category: Handa, N | + | [[Category: Handa, N]] |
| - | [[Category: Hirano, T | + | [[Category: Hirano, T]] |
| - | [[Category: Honda, K | + | [[Category: Honda, K]] |
| - | [[Category: Kagechika, H | + | [[Category: Kagechika, H]] |
| - | [[Category: Niwa, H | + | [[Category: Niwa, H]] |
| - | [[Category: Ohsawa, N | + | [[Category: Ohsawa, N]] |
| - | [[Category: Shirouzu, M | + | [[Category: Shirouzu, M]] |
| - | [[Category: Tomabechi, Y | + | [[Category: Tomabechi, Y]] |
| - | [[Category: Toyama, M | + | [[Category: Toyama, M]] |
| - | [[Category: Umehara, T | + | [[Category: Umehara, T]] |
| - | [[Category: Yokoyama, S | + | [[Category: Yokoyama, S]] |
[[Category: Adenosylmethionine binding]] | [[Category: Adenosylmethionine binding]] | ||
[[Category: Set domain]] | [[Category: Set domain]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
[[Category: Transferase-transferase inhibitor complex]] | [[Category: Transferase-transferase inhibitor complex]] | ||
Revision as of 20:09, 24 December 2014
Crystal structure of histone methyltransferase SET7/9 in comlex with DAAM-3
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