3smq: Difference between revisions

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<StructureSection load='3smq' size='340' side='right'caption='[[3smq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3smq' size='340' side='right'caption='[[3smq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3smq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SMQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SMQ FirstGlance]. <br>
<table><tr><td colspan='2'>[[3smq]] is a 1 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=3SMQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SMQ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=TDU:1-(1,2,3-BENZOTHIADIAZOL-6-YL)-3-[2-(CYCLOHEX-1-EN-1-YL)ETHYL]UREA'>TDU</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</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]] 2&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PRMT3, HRMT1L3 ([https://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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=TDU:1-(1,2,3-BENZOTHIADIAZOL-6-YL)-3-[2-(CYCLOHEX-1-EN-1-YL)ETHYL]UREA'>TDU</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</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=3smq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3smq OCA], [https://pdbe.org/3smq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3smq RCSB], [https://www.ebi.ac.uk/pdbsum/3smq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3smq ProSAT]</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=3smq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3smq OCA], [https://pdbe.org/3smq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3smq RCSB], [https://www.ebi.ac.uk/pdbsum/3smq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3smq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ANM3_HUMAN ANM3_HUMAN]] Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins.  
[https://www.uniprot.org/uniprot/ANM3_HUMAN ANM3_HUMAN] Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
PRMT3, a protein arginine methyltransferase, has been shown to influence ribosomal biosynthesis by catalyzing the dimethylation of the 40S ribosomal protein S2. Although PRMT3 has been reported to be a cytosolic protein, it has been shown to methylate histone H4 peptide (H4 1-24) in vitro. Here, we report the identification of a PRMT3 inhibitor (1-(benzo[d][1,2,3]thiadiazol-6-yl)-3-(2-cyclohexenylethyl)urea; compound 1) with IC50 value of 2.5 muM by screening a library of 16,000 compounds using H4 (1-24) peptide as a substrate. The crystal structure of PRMT3 in complex with compound 1 as well as kinetic analysis reveals an allosteric mechanism of inhibition. Mutating PRMT3 residues within the allosteric site or using compound 1 analogs that disrupt interactions with allosteric site residues both abrogated binding and inhibitory activity. These data demonstrate an allosteric mechanism for inhibition of protein arginine methyltransferases, an emerging class of therapeutic targets.
 
An allosteric inhibitor of protein arginine methyltransferase 3.,Siarheyeva A, Senisterra G, Allali-Hassani A, Dong A, Dobrovetsky E, Wasney GA, Chau I, Marcellus R, Hajian T, Liu F, Korboukh I, Smil D, Bolshan Y, Min J, Wu H, Zeng H, Loppnau P, Poda G, Griffin C, Aman A, Brown PJ, Jin J, Al-Awar R, Arrowsmith CH, Schapira M, Vedadi M Structure. 2012 Aug 8;20(8):1425-35. doi: 10.1016/j.str.2012.06.001. Epub 2012, Jul 12. PMID:22795084<ref>PMID:22795084</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3smq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Al-Awar, R]]
[[Category: Al-Awar R]]
[[Category: Allali-Hassani, A]]
[[Category: Allali-Hassani A]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith CH]]
[[Category: Bolshan, Y]]
[[Category: Bolshan Y]]
[[Category: Bountra, C]]
[[Category: Bountra C]]
[[Category: Brown, P J]]
[[Category: Brown PJ]]
[[Category: Dobrovetsky, E]]
[[Category: Dobrovetsky E]]
[[Category: Dong, A]]
[[Category: Dong A]]
[[Category: Edwards, A M]]
[[Category: Edwards AM]]
[[Category: Hajian, T]]
[[Category: Hajian T]]
[[Category: Nguyen, K T]]
[[Category: Nguyen KT]]
[[Category: Poda, G]]
[[Category: Poda G]]
[[Category: Structural genomic]]
[[Category: Schapira M]]
[[Category: Schapira, M]]
[[Category: Senisterra G]]
[[Category: Senisterra, G]]
[[Category: Siarheyeva A]]
[[Category: Siarheyeva, A]]
[[Category: Smil D]]
[[Category: Smil, D]]
[[Category: Vedadi M]]
[[Category: Vedadi, M]]
[[Category: Walker JR]]
[[Category: Walker, J R]]
[[Category: Wasney GA]]
[[Category: Wasney, G A]]
[[Category: Weigelt J]]
[[Category: Weigelt, J]]
[[Category: Prmt3]]
[[Category: Sgc]]
[[Category: Transferase]]

Latest revision as of 16:01, 14 March 2024

Crystal structure of protein arginine methyltransferase 3Crystal structure of protein arginine methyltransferase 3

Structural highlights

3smq is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ANM3_HUMAN Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins.

3smq, resolution 2.00Å

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