6taq
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Structure of the dArc2 capsid== | |
+ | <SX load='6taq' size='340' side='right' viewer='molstar' caption='[[6taq]], [[Resolution|resolution]] 3.90Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[6taq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TAQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TAQ FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.9Å</td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6taq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6taq OCA], [https://pdbe.org/6taq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6taq RCSB], [https://www.ebi.ac.uk/pdbsum/6taq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6taq ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [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] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | 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. | ||
- | + | 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> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 6taq" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </SX> | ||
+ | [[Category: Drosophila melanogaster]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Briggs JAG]] | ||
+ | [[Category: Erlendsson S]] | ||
+ | [[Category: Morado DR]] | ||
+ | [[Category: Shepherd JD]] |
Current revision
Structure of the dArc2 capsid
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