6xfm

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Current revision (14:49, 6 March 2024) (edit) (undo)
 
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<StructureSection load='6xfm' size='340' side='right'caption='[[6xfm]], [[Resolution|resolution]] 2.62&Aring;' scene=''>
<StructureSection load='6xfm' size='340' side='right'caption='[[6xfm]], [[Resolution|resolution]] 2.62&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6xfm]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XFM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6XFM FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6xfm]] is a 8 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=6XFM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XFM FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FUS, TLS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.62&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6xfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xfm OCA], [http://pdbe.org/6xfm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6xfm RCSB], [http://www.ebi.ac.uk/pdbsum/6xfm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6xfm ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6xfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xfm OCA], [https://pdbe.org/6xfm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xfm RCSB], [https://www.ebi.ac.uk/pdbsum/6xfm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xfm 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.
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ghosh, U]]
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[[Category: Ghosh U]]
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[[Category: Kato, M]]
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[[Category: Kato M]]
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[[Category: Lee, M]]
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[[Category: Lee M]]
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[[Category: Thurber, K]]
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[[Category: Thurber K]]
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[[Category: Tycko, R]]
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[[Category: Tycko R]]
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[[Category: Amyloid fibril]]
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[[Category: Low complexity domain]]
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[[Category: Protein aggregation]]
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[[Category: Protein fibril]]
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[[Category: Rna binding protein]]
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Current revision

Molecular structure of the core of amyloid-like fibrils formed by residues 111-214 of FUS

PDB ID 6xfm

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