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6tat

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(New page: '''Unreleased structure''' The entry 6tat is ON HOLD Authors: Description: Category: Unreleased Structures)
Current revision (11:09, 30 March 2022) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 6tat is ON HOLD
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==Structure of the five-fold capsomer of the dArc2 capsid==
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<SX load='6tat' size='340' side='right' viewer='molstar' caption='[[6tat]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6tat]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TAT FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Arc2, CG13941 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=6tat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tat OCA], [https://pdbe.org/6tat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tat RCSB], [https://www.ebi.ac.uk/pdbsum/6tat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tat ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/ARC2_DROME ARC2_DROME]] Self-assembles into virion-like capsids that encapsulate RNAs and mediate intercellular RNA transfer. Arc2 protein is released from cells in extracellular vesicles that mediate the transfer of mRNA into neighboring cells.[UniProtKB:Q7K1U0]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Arc, a neuronal gene that is critical for synaptic plasticity, originated through the domestication of retrotransposon Gag genes and mediates intercellular messenger RNA transfer. We report high-resolution structures of retrovirus-like capsids formed by Drosophila dArc1 and dArc2 that have surface spikes and putative internal RNA-binding domains. These data demonstrate that virus-like capsid-forming properties of Arc are evolutionarily conserved and provide a structural basis for understanding their function in intercellular communication.
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Authors:
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Structures of virus-like capsids formed by the Drosophila neuronal Arc proteins.,Erlendsson S, Morado DR, Cullen HB, Feschotte C, Shepherd JD, Briggs JAG Nat Neurosci. 2020 Feb;23(2):172-175. doi: 10.1038/s41593-019-0569-y. Epub 2020, Jan 6. PMID:31907439<ref>PMID:31907439</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6tat" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</SX>
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[[Category: Drome]]
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[[Category: Large Structures]]
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[[Category: Briggs, J A.G]]
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[[Category: Erlendsson, S]]
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[[Category: Morado, D R]]
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[[Category: Shepherd, J D]]
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[[Category: Darc]]
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[[Category: Gag]]
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[[Category: Virus]]
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[[Category: Virus like particle]]
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[[Category: Vlp]]

Current revision

Structure of the five-fold capsomer of the dArc2 capsid

6tat, resolution 3.70Å

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