5zgl

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<StructureSection load='5zgl' size='340' side='right'caption='[[5zgl]], [[Resolution|resolution]] 0.95&Aring;' scene=''>
<StructureSection load='5zgl' size='340' side='right'caption='[[5zgl]], [[Resolution|resolution]] 0.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5zgl]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZGL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZGL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5zgl]] 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=5ZGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZGL 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=5zgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zgl OCA], [http://pdbe.org/5zgl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zgl RCSB], [http://www.ebi.ac.uk/pdbsum/5zgl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zgl ProSAT]</span></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]] 0.95&#8491;</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=5zgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zgl OCA], [https://pdbe.org/5zgl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zgl RCSB], [https://www.ebi.ac.uk/pdbsum/5zgl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zgl ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/ROA1_HUMAN ROA1_HUMAN]] Amyotrophic lateral sclerosis;Inclusion body myopathy with Paget disease of bone and frontotemporal dementia. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:23455423</ref> The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:23455423</ref>
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[https://www.uniprot.org/uniprot/ROA1_HUMAN ROA1_HUMAN] Amyotrophic lateral sclerosis;Inclusion body myopathy with Paget disease of bone and frontotemporal dementia. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:23455423</ref> The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:23455423</ref>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ROA1_HUMAN ROA1_HUMAN]] Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may modulate splice site selection. May play a role in HCV RNA replication.<ref>PMID:17229681</ref>
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[https://www.uniprot.org/uniprot/ROA1_HUMAN ROA1_HUMAN] Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may modulate splice site selection. May play a role in HCV RNA replication.<ref>PMID:17229681</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Subcellular membrane-less organelles consist of proteins with low complexity domains. Many of them, such as hnRNPA1, can assemble into both a polydisperse liquid phase and an ordered solid phase of amyloid fibril. The former mirrors biological granule assembly, while the latter is usually associated with neurodegenerative disease. Here, we observe a reversible amyloid formation of hnRNPA1 that synchronizes with liquid-liquid phase separation, regulates the fluidity and mobility of the liquid-like droplets, and facilitates the recruitment of hnRNPA1 into stress granules. We identify the reversible amyloid-forming cores of hnRNPA1 (named hnRACs). The atomic structures of hnRACs reveal a distinct feature of stacking Asp residues, which contributes to fibril reversibility and explains the irreversible pathological fibril formation caused by the Asp mutations identified in familial ALS. Our work characterizes the structural diversity and heterogeneity of reversible amyloid fibrils and illuminates the biological function of reversible amyloid formation in protein phase separation.
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Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly.,Gui X, Luo F, Li Y, Zhou H, Qin Z, Liu Z, Gu J, Xie M, Zhao K, Dai B, Shin WS, He J, He L, Jiang L, Zhao M, Sun B, Li X, Liu C, Li D Nat Commun. 2019 May 1;10(1):2006. doi: 10.1038/s41467-019-09902-7. PMID:31043593<ref>PMID:31043593</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 5zgl" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Gui, X]]
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[[Category: Gui X]]
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[[Category: He, J]]
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[[Category: He J]]
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[[Category: Li, D]]
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[[Category: Li D]]
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[[Category: Liu, C]]
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[[Category: Liu C]]
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[[Category: Luo, F]]
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[[Category: Luo F]]
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[[Category: Xie, M]]
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[[Category: Xie M]]
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[[Category: Zhao, M]]
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[[Category: Zhao M]]
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[[Category: Phase separation]]
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[[Category: Reversibility]]
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[[Category: Rna binding protein]]
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Current revision

hnRNP A1 segment GGGYGGS (residues 234-240)

PDB ID 5zgl

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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