View source for 7fbr


==Solution structure of The first RNA binding domain of Matrin-3==
<StructureSection load='7fbr' size='340' side='right'caption='[[7fbr]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7fbr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7FBR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FBR FirstGlance]. <br>
</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=7fbr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7fbr OCA], [https://pdbe.org/7fbr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7fbr RCSB], [https://www.ebi.ac.uk/pdbsum/7fbr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7fbr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MATR3_MOUSE MATR3_MOUSE] May play a role in transcription or may interact with other nuclear matrix proteins to form the internal fibrogranular network. In association with the SFPQ-NONO heteromer may play a role in nuclear retention of defective RNAs (By similarity).
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== Publication Abstract from PubMed ==
Matrin-3 is a multifunctional protein that binds to both DNA and RNA. Its DNA-binding activity is linked to the formation of the nuclear matrix and transcriptional regulation, while its RNA-binding activity is linked to mRNA metabolism including splicing, transport, stabilization, and degradation. Correspondingly, Matrin-3 has two zinc finger domains for DNA binding and two consecutive RNA recognition motif (RRM) domains for RNA binding. Matrin-3 has been reported to cause amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) when its disordered region contains pathogenic mutations. Simultaneously, it has been shown that the RNA-binding activity of Matrin-3 mediated by its RRM domains, affects the formation of insoluble cytoplasmic granules, which are related to the pathogenic mechanism of ALS/FTD. Thus, the effect of the RRM domains on the phase separation of condensed protein/RNA mixtures has to be clarified for a comprehensive understanding of ALS/FTD. Here, we report the (1)H, (15)N, and (13)C resonance assignments of the two RNA binding domains and their solution structures. The resonance assignments and the solution structures obtained in this work will contribute to the elucidation of the molecular basis of Matrin-3 in the pathogenic mechanism of ALS and/or FTD.

(1)H, (13)C and (15)N resonance assignments and solution structures of the two RRM domains of Matrin-3.,He F, Kuwasako K, Takizawa M, Takahashi M, Tsuda K, Nagata T, Watanabe S, Tanaka A, Kobayashi N, Kigawa T, Guntert P, Shirouzu M, Yokoyama S, Muto Y Biomol NMR Assign. 2021 Nov 16. pii: 10.1007/s12104-021-10057-0. doi:, 10.1007/s12104-021-10057-0. PMID:34783967<ref>PMID:34783967</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7fbr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Kobayashi N]]
[[Category: Muto Y]]
[[Category: Yokoyama S]]