View source for 2mtv


==Solution Structure of the YTH Domain of YT521-B in complex with N6-Methyladenosine containing RNA==
<StructureSection load='2mtv' size='340' side='right'caption='[[2mtv]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mtv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MTV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MTV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR,  models</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6MZ:N6-METHYLADENOSINE-5-MONOPHOSPHATE'>6MZ</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=2mtv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mtv OCA], [https://pdbe.org/2mtv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mtv RCSB], [https://www.ebi.ac.uk/pdbsum/2mtv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mtv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/YTDC1_RAT YTDC1_RAT] RNA-binding protein that regulates alternative splice site selection.<ref>PMID:10564280</ref> <ref>PMID:9473574</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
N6A methylation is the most abundant RNA modification occurring within messenger RNA. Impairment of methylase or demethylase functions are associated with severe phenotypes and diseases in several organisms. Beside writer and eraser enzymes of this dynamic RNA epigenetic modification, reader proteins that recognize this modification are involved in numerous cellular processes. Although the precise characterization of these reader proteins remains unknown, preliminary data showed that most potential reader proteins contained a conserved YT521-B homology (YTH) domain. Here we define the YTH domain of rat YT521-B as a N6-methylated adenosine reader domain and report its solution structure in complex with a N6-methylated RNA. The structure reveals a binding preference for NGANNN RNA hexamer and a deep hydrophobic cleft for m6A recognition. These findings establish a molecular function for YTH domains as m6A reader domains and should guide further studies into the biological functions of YTH-containing proteins in m6A recognition.

Solution structure of the YTH domain in complex with N6-methyladenosine RNA: a reader of methylated RNA.,Theler D, Dominguez C, Blatter M, Boudet J, Allain FH Nucleic Acids Res. 2014 Nov 11. pii: gku1116. PMID:25389274<ref>PMID:25389274</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mtv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Synthetic construct]]
[[Category: Allain FH-T]]
[[Category: Blatter M]]
[[Category: Boudet J]]
[[Category: Dominguez C]]
[[Category: Theler D]]