5fqn
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of M. musculus protein arginine methyltransferase PRMT6 with SAH at 1.65 Angstroms== | |
| + | <StructureSection load='5fqn' size='340' side='right'caption='[[5fqn]], [[Resolution|resolution]] 1.66Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5fqn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FQN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FQN FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.657Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></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=5fqn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fqn OCA], [https://pdbe.org/5fqn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fqn RCSB], [https://www.ebi.ac.uk/pdbsum/5fqn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fqn ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ANM6_MOUSE ANM6_MOUSE] Arginine methyltransferase that can catalyze the formation of both omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA), with a strong preference for the formation of aDMA. Preferentially methylates arginyl residues present in a glycine and arginine-rich domain and displays preference for monomethylated substrates. Specifically mediates the asymmetric dimethylation of histone H3 'Arg-2' to form H3R2me2a. H3R2me2a represents a specific tag for epigenetic transcriptional repression and is mutually exclusive with methylation on histone H3 'Lys-4' (H3K4me2 and H3K4me3). Acts as a transcriptional repressor of various genes such as HOXA2, THBS1 and TP53. Repression of TP53 blocks cellular senescence. Also methylates histone H2A and H4 'Arg-3' (H2AR3me and H4R3me, respectively). Acts as a regulator of DNA base excision during DNA repair by mediating the methylation of DNA polymerase beta (POLB), leading to the stimulation of its polymerase activity by enhancing DNA binding and processivity. Methylates HMGA1. Regulates alternative splicing events. Acts as a transcriptional coactivator of a number of steroid hormone receptors including ESR1, ESR2, PGR and NR3C1. Promotes fasting-induced transcriptional activation of the gluconeogenic program through methylation of the CRTC2 transcription coactivator.<ref>PMID:22904064</ref> <ref>PMID:24570487</ref> | ||
| - | + | ==See Also== | |
| - | + | *[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]] | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: Bonnefond | + | </StructureSection> |
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Bonnefond L]] | ||
| + | [[Category: Cavarelli J]] | ||
Current revision
Crystal structure of M. musculus protein arginine methyltransferase PRMT6 with SAH at 1.65 Angstroms
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