5xrr

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==Crystal structure of FUS (54-59) SYSSYG==
==Crystal structure of FUS (54-59) SYSSYG==
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<StructureSection load='5xrr' size='340' side='right' caption='[[5xrr]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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<StructureSection load='5xrr' size='340' side='right'caption='[[5xrr]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5xrr]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XRR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XRR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5xrr]] is a 1 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=5XRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XRR FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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">X-ray diffraction, [[Resolution|Resolution]] 1.503&#8491;</td></tr>
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<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=5xrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xrr OCA], [http://pdbe.org/5xrr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xrr RCSB], [http://www.ebi.ac.uk/pdbsum/5xrr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xrr ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5xrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xrr OCA], [https://pdbe.org/5xrr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xrr RCSB], [https://www.ebi.ac.uk/pdbsum/5xrr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xrr 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: Gui, X]]
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[[Category: Homo sapiens]]
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[[Category: Li, D]]
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[[Category: Large Structures]]
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[[Category: Liu, C]]
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[[Category: Gui X]]
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[[Category: Zhao, M]]
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[[Category: Li D]]
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[[Category: Hydrous amyloid fibril spine]]
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[[Category: Liu C]]
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[[Category: Low complexity domain]]
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[[Category: Zhao M]]
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[[Category: Reversible amyloid]]
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[[Category: Rna binding protein]]
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[[Category: Rna granule assembly]]
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Current revision

Crystal structure of FUS (54-59) SYSSYG

PDB ID 5xrr

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