2lv9
From Proteopedia
(Difference between revisions)
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==Solution NMR structure of the PHD domain of human MLL5, Northeast structural genomics consortium target HR6512A== | ==Solution NMR structure of the PHD domain of human MLL5, Northeast structural genomics consortium target HR6512A== | ||
| - | <StructureSection load='2lv9' size='340' side='right' caption='[[2lv9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2lv9' size='340' side='right'caption='[[2lv9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2lv9]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2lv9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LV9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LV9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MLL5, KMT2E ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MLL5, KMT2E ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lv9 OCA], [https://pdbe.org/2lv9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lv9 RCSB], [https://www.ebi.ac.uk/pdbsum/2lv9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lv9 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/MLL5_HUMAN MLL5_HUMAN]] Histone methyltransferase that specifically mono- and dimethylates 'Lys-4' of histone H3 (H3K4me1 and H3K4me2). H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Key regulator of hematopoiesis involved in terminal myeloid differentiation and in the regulation of hematopoietic stem cell (HSCs) self-renewal by a mechanism that involves DNA methylation. Plays an essential role in retinoic-acid-induced granulopoiesis by acting as a coactivator of RAR-alpha (RARA) in target gene promoters. Also acts as an important cell cycle regulator, participating in cell cycle regulatory network machinery at multiple cell cycle stages. Required to suppress inappropriate expression of S-phase-promoting genes and maintain expression of determination genes in quiescent cells. Overexpression inhibits cell cycle progression, while knockdown induces cell cycle arrest at both the G1 and G2/M phases.<ref>PMID:14718661</ref> <ref>PMID:18573682</ref> <ref>PMID:19377461</ref> |
==See Also== | ==See Also== | ||
| - | *[[Histone methyltransferase|Histone methyltransferase]] | + | *[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Histone-lysine N-methyltransferase]] | [[Category: Histone-lysine N-methyltransferase]] | ||
[[Category: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Arrowsmith, C]] | [[Category: Arrowsmith, C]] | ||
[[Category: CEBS, Chaperone-Enabled Studies of Epigenetic Regulation Enzymes]] | [[Category: CEBS, Chaperone-Enabled Studies of Epigenetic Regulation Enzymes]] | ||
Revision as of 10:54, 19 May 2021
Solution NMR structure of the PHD domain of human MLL5, Northeast structural genomics consortium target HR6512A
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Categories: Histone-lysine N-methyltransferase | Human | Large Structures | Arrowsmith, C | CEBS, Chaperone-Enabled Studies of Epigenetic Regulation Enzymes | Garcia, M | Houliston, S | Lemak, A | Min, J | Montelione, G T | Structural genomic | Wu, H | Yee, A | Ceb | Chaperone-enabled studies of epigenetic regulation enzyme | Nesg | Protein binding | Psi-biology | Sgc | Transcription | Transferase | Zinc finger
