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| | <StructureSection load='6ago' size='340' side='right'caption='[[6ago]], [[Resolution|resolution]] 3.10Å' scene=''> | | <StructureSection load='6ago' size='340' side='right'caption='[[6ago]], [[Resolution|resolution]] 3.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ago]] 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=6AGO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AGO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ago]] 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=6AGO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AGO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.103Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ASH1L, KIAA1420, KMT2H ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), MORF4L1, MRG15, FWP006, HSPC008, HSPC061, PP368 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=6ago FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ago OCA], [https://pdbe.org/6ago PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ago RCSB], [https://www.ebi.ac.uk/pdbsum/6ago PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ago ProSAT]</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=6ago FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ago OCA], [http://pdbe.org/6ago PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ago RCSB], [http://www.ebi.ac.uk/pdbsum/6ago PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ago ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ASH1L_HUMAN ASH1L_HUMAN]] Histone methyltransferase specifically methylating 'Lys-36' of histone H3 (H3K36me).<ref>PMID:21239497</ref> | + | [https://www.uniprot.org/uniprot/ASH1L_HUMAN ASH1L_HUMAN] Histone methyltransferase specifically methylating 'Lys-36' of histone H3 (H3K36me).<ref>PMID:21239497</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Human ASH1L is the catalytic subunit of the conserved histone methyltransferase (HMTase) complex AMC that dimethylates lysine 36 in histone H3 (H3K36me2) to promote gene transcription in mammals and flies. Unlike AMC, ASH1L alone shows poor catalytic activity, because access to its substrate binding pocket is blocked by an autoinhibitory loop (AI loop) from the postSET domain. We report the crystal structure of the minimal catalytic active AMC complex containing ASH1L and its partner subunit MRG15. The structure reveals how binding of the MRG domain of MRG15 to a conserved FxLP motif in ASH1L results in the displacement of the AI loop to permit substrates to access the catalytic pocket of the ASH1L SET domain. Together, ASH1L activation by MRG15 therefore represents a delicate regulatory mechanism for how a cofactor activates an SET domain HMTase by releasing autoinhibition.
| + | |
| | | | |
| - | Structural Basis of MRG15-Mediated Activation of the ASH1L Histone Methyltransferase by Releasing an Autoinhibitory Loop.,Lee Y, Yoon E, Cho S, Schmahling S, Muller J, Song JJ Structure. 2019 Feb 9. pii: S0969-2126(19)30016-4. doi:, 10.1016/j.str.2019.01.016. PMID:30827841<ref>PMID:30827841</ref>
| + | ==See Also== |
| - | | + | *[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]] |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 6ago" style="background-color:#fffaf0;"></div>
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Histone-lysine N-methyltransferase]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lee, Y]] | + | [[Category: Lee Y]] |
| - | [[Category: Song, J]] | + | [[Category: Song J]] |
| - | [[Category: Activation]]
| + | |
| - | [[Category: Gene regulation]]
| + | |
| - | [[Category: Methylation]]
| + | |
| - | [[Category: Nucleosome]]
| + | |
| - | [[Category: Regulation]]
| + | |
| - | [[Category: Transferase-gene regulation complex]]
| + | |
