5w3n

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==Molecular structure of FUS low sequence complexity domain protein fibrils==
==Molecular structure of FUS low sequence complexity domain protein fibrils==
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<StructureSection load='5w3n' size='340' side='right' caption='[[5w3n]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='5w3n' size='340' side='right'caption='[[5w3n]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5w3n]] is a 9 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W3N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5W3N FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5w3n]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W3N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5W3N FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5w3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w3n OCA], [http://pdbe.org/5w3n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5w3n RCSB], [http://www.ebi.ac.uk/pdbsum/5w3n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5w3n ProSAT]</span></td></tr>
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</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=5w3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w3n OCA], [https://pdbe.org/5w3n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5w3n RCSB], [https://www.ebi.ac.uk/pdbsum/5w3n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5w3n ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/FUS_HUMAN FUS_HUMAN]] Frontotemporal dementia with motor neuron disease;Hereditary essential tremor;Amyotrophic lateral sclerosis;Juvenile amyotrophic lateral sclerosis;Myxofibrosarcoma;Myxoid/round cell liposarcoma. A chromosomal aberration involving FUS is found in a patient with malignant myxoid liposarcoma. Translocation t(12;16)(q13;p11) with DDIT3. A chromosomal aberration involving FUS is a cause of acute myeloid leukemia (AML). Translocation t(16;21)(p11;q22) with ERG. The disease may be caused by mutations affecting the gene represented in this entry. A chromosomal aberration involving FUS is found in a patient with angiomatoid fibrous histiocytoma. Translocation t(12;16)(q13;p11.2) with ATF1 generates a chimeric FUS/ATF1 protein. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/FUS_HUMAN FUS_HUMAN] Frontotemporal dementia with motor neuron disease;Hereditary essential tremor;Amyotrophic lateral sclerosis;Juvenile amyotrophic lateral sclerosis;Myxofibrosarcoma;Myxoid/round cell liposarcoma. A chromosomal aberration involving FUS is found in a patient with malignant myxoid liposarcoma. Translocation t(12;16)(q13;p11) with DDIT3. A chromosomal aberration involving FUS is a cause of acute myeloid leukemia (AML). Translocation t(16;21)(p11;q22) with ERG. The disease may be caused by mutations affecting the gene represented in this entry. A chromosomal aberration involving FUS is found in a patient with angiomatoid fibrous histiocytoma. Translocation t(12;16)(q13;p11.2) with ATF1 generates a chimeric FUS/ATF1 protein. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/FUS_HUMAN FUS_HUMAN]] Binds both single-stranded and double-stranded DNA and promotes ATP-independent annealing of complementary single-stranded DNAs and D-loop formation in superhelical double-stranded DNA. May play a role in maintenance of genomic integrity.
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[https://www.uniprot.org/uniprot/FUS_HUMAN FUS_HUMAN] Binds both single-stranded and double-stranded DNA and promotes ATP-independent annealing of complementary single-stranded DNAs and D-loop formation in superhelical double-stranded DNA. May play a role in maintenance of genomic integrity.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Polymerization and phase separation of proteins containing low-complexity (LC) domains are important factors in gene expression, mRNA processing and trafficking, and localization of translation. We have used solid-state nuclear magnetic resonance methods to characterize the molecular structure of self-assembling fibrils formed by the LC domain of the fused in sarcoma (FUS) RNA-binding protein. From the 214-residue LC domain of FUS (FUS-LC), a segment of only 57 residues forms the fibril core, while other segments remain dynamically disordered. Unlike pathogenic amyloid fibrils, FUS-LC fibrils lack hydrophobic interactions within the core and are not polymorphic at the molecular structural level. Phosphorylation of core-forming residues by DNA-dependent protein kinase blocks binding of soluble FUS-LC to FUS-LC hydrogels and dissolves phase-separated, liquid-like FUS-LC droplets. These studies offer a structural basis for understanding LC domain self-assembly, phase separation, and regulation by post-translational modification.
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Structure of FUS Protein Fibrils and Its Relevance to Self-Assembly and Phase Separation of Low-Complexity Domains.,Murray DT, Kato M, Lin Y, Thurber KR, Hung I, McKnight SL, Tycko R Cell. 2017 Oct 19;171(3):615-627.e16. doi: 10.1016/j.cell.2017.08.048. Epub 2017 , Sep 21. PMID:28942918<ref>PMID:28942918</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5w3n" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Hung, I]]
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[[Category: Homo sapiens]]
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[[Category: Kato, M]]
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[[Category: Large Structures]]
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[[Category: Lin, Y]]
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[[Category: Hung I]]
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[[Category: McKnight, S]]
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[[Category: Kato M]]
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[[Category: Murray, D T]]
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[[Category: Lin Y]]
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[[Category: Thurber, K]]
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[[Category: McKnight S]]
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[[Category: Tycko, R]]
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[[Category: Murray DT]]
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[[Category: Intrinsically disordered protein]]
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[[Category: Thurber K]]
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[[Category: Low complexity sequence domain]]
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[[Category: Tycko R]]
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[[Category: Protein fibril]]
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[[Category: Rna granule]]
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[[Category: Rna transport]]
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Current revision

Molecular structure of FUS low sequence complexity domain protein fibrils

PDB ID 5w3n

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