6bxx

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Current revision (14:24, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6bxx' size='340' side='right'caption='[[6bxx]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
<StructureSection load='6bxx' size='340' side='right'caption='[[6bxx]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6bxx]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BXX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BXX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6bxx]] 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=6BXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BXX 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=6bxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bxx OCA], [http://pdbe.org/6bxx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bxx RCSB], [http://www.ebi.ac.uk/pdbsum/6bxx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bxx 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]] 1.1&#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=6bxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bxx OCA], [https://pdbe.org/6bxx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bxx RCSB], [https://www.ebi.ac.uk/pdbsum/6bxx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bxx ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Disease ==
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== Publication Abstract from PubMed ==
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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>
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Subcellular membraneless assemblies are a reinvigorated area of study in biology, with spirited scientific discussions on the forces between the low-complexity protein domains within these assemblies. To illuminate these forces, we determined the atomic structures of five segments from protein low-complexity domains associated with membraneless assemblies. Their common structural feature is the stacking of segments into kinked beta sheets that pair into protofilaments. Unlike steric zippers of amyloid fibrils, the kinked sheets interact weakly through polar atoms and aromatic side chains. By computationally threading the human proteome on our kinked structures, we identified hundreds of low-complexity segments potentially capable of forming such interactions. These segments are found in proteins as diverse as RNA binders, nuclear pore proteins, and keratins, which are known to form networks and localize to membraneless assemblies.
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== Function ==
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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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Atomic structures of low-complexity protein segments reveal kinked beta sheets that assemble networks.,Hughes MP, Sawaya MR, Boyer DR, Goldschmidt L, Rodriguez JA, Cascio D, Chong L, Gonen T, Eisenberg DS Science. 2018 Feb 9;359(6376):698-701. doi: 10.1126/science.aan6398. PMID:29439243<ref>PMID:29439243</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 6bxx" 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: Cascio, D]]
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[[Category: Cascio D]]
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[[Category: Eisenberg, D S]]
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[[Category: Eisenberg DS]]
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[[Category: Gonen, T]]
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[[Category: Gonen T]]
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[[Category: Hughes, M P]]
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[[Category: Hughes MP]]
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[[Category: Rodriguez, J A]]
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[[Category: Rodriguez JA]]
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[[Category: Sawaya, M R]]
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[[Category: Sawaya MR]]
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[[Category: Amyloid]]
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[[Category: Lark]]
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[[Category: Low-complexity]]
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[[Category: Protein fibril]]
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[[Category: Reversible-amyloid]]
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Current revision

GYNGFG from low-complexity domain of hnRNPA1, residues 243-248

PDB ID 6bxx

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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