6fdl: Difference between revisions

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'''Unreleased structure'''


The entry 6fdl is ON HOLD
==Crystal structure of the NYN domain of human MARF1==
<StructureSection load='6fdl' size='340' side='right'caption='[[6fdl]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6fdl]] is a 2 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=6FDL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FDL 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]] 1.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=6fdl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fdl OCA], [https://pdbe.org/6fdl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fdl RCSB], [https://www.ebi.ac.uk/pdbsum/6fdl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fdl ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Meiosis arrest female 1 (MARF1) is a cytoplasmic RNA binding protein that is essential for meiotic progression of mouse oocytes, in part by limiting retrotransposon expression. MARF1 is also expressed in somatic cells and tissues; however, its mechanism of action has yet to be investigated. Human MARF1 contains a NYN-like domain, two RRMs and eight LOTUS domains. Here we provide evidence that MARF1 post-transcriptionally silences targeted mRNAs. MARF1 physically interacts with the DCP1:DCP2 mRNA decapping complex but not with deadenylation machineries. Importantly, we provide a 1.7 A resolution crystal structure of the human MARF1 NYN domain, which we demonstrate is a bona fide endoribonuclease, the activity of which is essential for the repression of MARF1-targeted mRNAs. Thus, MARF1 post-transcriptionally represses gene expression by serving as both an endoribonuclease and as a platform that recruits the DCP1:DCP2 decapping complex to targeted mRNAs.


Authors: Jinek, M., Brandmann, T.
Human MARF1 is an endoribonuclease that interacts with the DCP1:2 decapping complex and degrades target mRNAs.,Nishimura T, Fakim H, Brandmann T, Youn JY, Gingras AC, Jinek M, Fabian MR Nucleic Acids Res. 2018 Oct 26. pii: 5144954. doi: 10.1093/nar/gky1011. PMID:30364987<ref>PMID:30364987</ref>


Description: Crystal structure of the NYN domain of human MARF1
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Jinek, M]]
<div class="pdbe-citations 6fdl" style="background-color:#fffaf0;"></div>
[[Category: Brandmann, T]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Brandmann T]]
[[Category: Jinek M]]
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