We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.
1urz
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1urz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1urz, resolution 2.7Å" /> '''LOW PH INDUCED, MEMBR...) |
|||
| (16 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:1urz.gif|left|200px]]<br /><applet load="1urz" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1urz, resolution 2.7Å" /> | ||
| - | '''LOW PH INDUCED, MEMBRANE FUSION CONFORMATION OF THE ENVELOPE PROTEIN OF TICK-BORNE ENCEPHALITIS VIRUS'''<br /> | ||
| - | == | + | ==Low pH induced, membrane fusion conformation of the envelope protein of tick-borne encephalitis virus== |
| - | Enveloped viruses enter cells via a membrane fusion reaction driven by | + | <StructureSection load='1urz' size='340' side='right'caption='[[1urz]], [[Resolution|resolution]] 2.70Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1urz]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Tick-borne_encephalitis_virus_(WESTERN_SUBTYPE) Tick-borne encephalitis virus (WESTERN SUBTYPE)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1URZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1URZ FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</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=1urz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1urz OCA], [https://pdbe.org/1urz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1urz RCSB], [https://www.ebi.ac.uk/pdbsum/1urz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1urz ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q80E47_9FLAV Q80E47_9FLAV] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ur/1urz_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1urz ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Enveloped viruses enter cells via a membrane fusion reaction driven by conformational changes of specific viral envelope proteins. We report here the structure of the ectodomain of the tick-borne encephalitis virus envelope glycoprotein, E, a prototypical class II fusion protein, in its trimeric low-pH-induced conformation. We show that, in the conformational transition, the three domains of the neutral-pH form are maintained but their relative orientation is altered. Similar to the postfusion class I proteins, the subunits rearrange such that the fusion peptide loops cluster at one end of an elongated molecule and the C-terminal segments, connecting to the viral transmembrane region, run along the sides of the trimer pointing toward the fusion peptide loops. Comparison with the low-pH-induced form of the alphavirus class II fusion protein reveals striking differences at the end of the molecule bearing the fusion peptides, suggesting an important conformational effect of the missing membrane connecting segment. | ||
| - | + | Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation.,Bressanelli S, Stiasny K, Allison SL, Stura EA, Duquerroy S, Lescar J, Heinz FX, Rey FA EMBO J. 2004 Feb 25;23(4):728-38. Epub 2004 Feb 12. PMID:14963486<ref>PMID:14963486</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 1urz" style="background-color:#fffaf0;"></div> |
| - | + | == References == | |
| - | [[Category: Bressanelli | + | <references/> |
| - | [[Category: Rey | + | __TOC__ |
| - | + | </StructureSection> | |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Bressanelli S]] | |
| - | + | [[Category: Rey FA]] | |
| - | + | ||
Current revision
Low pH induced, membrane fusion conformation of the envelope protein of tick-borne encephalitis virus
| |||||||||||
