View source for 5lgp


==Crystal structure of mouse CARM1 in complex with ligand P1C3s==
<StructureSection load='5lgp' size='340' side='right'caption='[[5lgp]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lgp]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LGP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LGP 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]] 2.04&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8ZB:(2~{R},3~{R},4~{S},5~{R})-2-(6-AMINOPURIN-9-YL)-5-PROPYL-OXOLANE-3,4-DIOL'>8ZB</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=5lgp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lgp OCA], [https://pdbe.org/5lgp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lgp RCSB], [https://www.ebi.ac.uk/pdbsum/5lgp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lgp ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Coactivator associated arginine methyltransferase 1 (CARM1) is a member of the protein arginine methyltransferase (PRMT) family and methylates a range of proteins in eukaryotic cells. Overexpression of CARM1 is implicated in a number of cancers, and it is therefore seen as a potential therapeutic target. Peptide sequences derived from the well-defined CARM1 substrate poly(A)-binding protein 1 (PABP1) were covalently linked to an adenosine moiety as in the AdoMet cofactor to generate transition state mimics. These constructs were found to be potent CARM1 inhibitors and also formed stable complexes with the enzyme. High-resolution crystal structures of CARM1 in complex with these compounds confirm a mode of binding that is indeed reflective of the transition state at the CARM1 active site. Given the transient nature of PRMT-substrate complexes, such transition state mimics represent valuable chemical tools for structural studies aimed at deciphering the regulation of arginine methylation mediated by the family of arginine methyltransferases.

Transition state mimics are valuable mechanistic probes for structural studies with the arginine methyltransferase CARM1.,van Haren MJ, Marechal N, Troffer-Charlier N, Cianciulli A, Sbardella G, Cavarelli J, Martin NI Proc Natl Acad Sci U S A. 2017 Mar 22. pii: 201618401. doi:, 10.1073/pnas.1618401114. PMID:28330993<ref>PMID:28330993</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5lgp" style="background-color:#fffaf0;"></div>

==See Also==
*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Bonnefond L]]
[[Category: Cavarelli J]]
[[Category: Cura V]]
[[Category: Marechal N]]
[[Category: Troffer-Charlier N]]