2mm4
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of a Conserved Golgi Complex-targeting Signal in Coronavirus Envelope Proteins== | |
| + | <StructureSection load='2mm4' size='340' side='right'caption='[[2mm4]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2mm4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Severe_acute_respiratory_syndrome-related_coronavirus Severe acute respiratory syndrome-related coronavirus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MM4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MM4 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2mm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mm4 OCA], [https://pdbe.org/2mm4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mm4 RCSB], [https://www.ebi.ac.uk/pdbsum/2mm4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mm4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/VEMP_SARS VEMP_SARS] Plays a central role in virus morphogenesis and assembly. Acts as a viroporin and self-assembles in host membranes forming pentameric protein-lipid pores that allow ion transport. Also plays a role in the induction of apoptosis (By similarity). Activates the host NLRP3 inflammasome, leading to IL-1beta overproduction.[HAMAP-Rule:MF_04204]<ref>PMID:24788150</ref> <ref>PMID:26331680</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Coronavirus envelope (CoV E) proteins are approximately 100-residue polypeptides with at least one channel-forming alpha-helical transmembrane (TM) domain. The extramembrane C-terminal tail contains a completely conserved proline, at the center of a predicted beta-coil-beta motif. This hydrophobic motif has been reported to constitute a Golgi-targeting signal or a second TM domain. However, no structural data for this or other extramembrane domains in CoV E proteins is available. Herein, we show that the E protein in the severe acute respiratory syndrome virus has only one TM domain in micelles, whereas the predicted beta-coil-beta motif forms a short membrane-bound alpha-helix connected by a disordered loop to the TM domain. However, complementary results suggest that this motif is potentially poised for conformational change or in dynamic exchange with other conformations. | ||
| - | + | Structure of a conserved Golgi complex-targeting signal in coronavirus envelope proteins.,Li Y, Surya W, Claudine S, Torres J J Biol Chem. 2014 May 2;289(18):12535-49. doi: 10.1074/jbc.M114.560094. Epub 2014, Mar 25. PMID:24668816<ref>PMID:24668816</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2mm4" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Severe acute respiratory syndrome-related coronavirus]] | ||
| + | [[Category: Claudine S]] | ||
| + | [[Category: Li Y]] | ||
| + | [[Category: Surya W]] | ||
| + | [[Category: Torres J]] | ||
Current revision
Structure of a Conserved Golgi Complex-targeting Signal in Coronavirus Envelope Proteins
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