5u4x: Difference between revisions

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==Coactivator-associated arginine methyltransferase 1==
==Coactivator-associated arginine methyltransferase 1 with TP-064==
<StructureSection load='5u4x' size='340' side='right' caption='[[5u4x]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
<StructureSection load='5u4x' size='340' side='right' caption='[[5u4x]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5u4x]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U4X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5U4X FirstGlance]. <br>
<table><tr><td colspan='2'>[[5u4x]] 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=5U4X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5U4X FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7VM:N-METHYL-N-[(2-{1-[2-(METHYLAMINO)ETHYL]PIPERIDIN-4-YL}PYRIDIN-4-YL)METHYL]-3-PHENOXYBENZAMIDE'>7VM</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7VM:N-METHYL-N-[(2-{1-[2-(METHYLAMINO)ETHYL]PIPERIDIN-4-YL}PYRIDIN-4-YL)METHYL]-3-PHENOXYBENZAMIDE'>7VM</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CARM1, PRMT4 ([http://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'>[http://en.wikipedia.org/wiki/Type_I_protein_arginine_methyltransferase Type I protein arginine methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.319 2.1.1.319] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Type_I_protein_arginine_methyltransferase Type I protein arginine methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.319 2.1.1.319] </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=5u4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u4x OCA], [http://pdbe.org/5u4x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5u4x RCSB], [http://www.ebi.ac.uk/pdbsum/5u4x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5u4x 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=5u4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u4x OCA], [http://pdbe.org/5u4x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5u4x RCSB], [http://www.ebi.ac.uk/pdbsum/5u4x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5u4x ProSAT]</span></td></tr>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Type I protein arginine methyltransferase]]
[[Category: Type I protein arginine methyltransferase]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith, C H]]
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[[Category: DONG, A]]
[[Category: DONG, A]]
[[Category: Edwards, A M]]
[[Category: Edwards, A M]]
[[Category: Hutchinson, A]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: STONE, H]]
[[Category: STONE, H]]
[[Category: Saikatendu, K S]]
[[Category: Saikatendu, K S]]
[[Category: Seitova, A]]
[[Category: WALKER, J R]]
[[Category: WALKER, J R]]
[[Category: WU, H]]
[[Category: WU, H]]

Revision as of 23:47, 24 January 2018

Coactivator-associated arginine methyltransferase 1 with TP-064Coactivator-associated arginine methyltransferase 1 with TP-064

Structural highlights

5u4x is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Gene:CARM1, PRMT4 (HUMAN)
Activity:Type I protein arginine methyltransferase, with EC number 2.1.1.319
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CARM1_HUMAN] Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability. Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activate transcription via chromatin remodeling. During nuclear hormone receptor activation and TCF7L2/TCF4 activation, acts synergically with EP300/P300 and either one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription. During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C. During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-kappa-B. Acts as coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue. Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors. Also seems to be involved in p53/TP53 transcriptional activation. Methylates EP300/P300, both at 'Arg-2142', which may loosen its interaction with NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation. Also methylates arginine residues in RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA-stabilizing properties and the half-life of their target mRNAs.[1] [2]

References

  1. Miao F, Li S, Chavez V, Lanting L, Natarajan R. Coactivator-associated arginine methyltransferase-1 enhances nuclear factor-kappaB-mediated gene transcription through methylation of histone H3 at arginine 17. Mol Endocrinol. 2006 Jul;20(7):1562-73. Epub 2006 Feb 23. PMID:16497732 doi:me.2005-0365
  2. Lakowski TM, Frankel A. Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4. Biochem J. 2009 Jun 26;421(2):253-61. doi: 10.1042/BJ20090268. PMID:19405910 doi:10.1042/BJ20090268

5u4x, resolution 1.88Å

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