6tat: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 6tat is ON HOLD
+==Structure of the five-fold capsomer of the dArc2 capsid==
+<SX load='6tat' size='340' side='right' viewer='molstar' caption='[[6tat]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6tat]] is a 5 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=6TAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TAT 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]] 3.7&#8491;</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=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>
+</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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6tat" 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]]