4jgs
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4jgs is ON HOLD Authors: Aydin, H, Cook, J.D., Smrke, B.M., Lee, J.E. Description: Crystal structure of a murine retroviral protein) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the xmrv tm retroviral fusion core== | |
| + | <StructureSection load='4jgs' size='340' side='right'caption='[[4jgs]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4jgs]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JGS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JGS 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]] 2.2Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=4jgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jgs OCA], [https://pdbe.org/4jgs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jgs RCSB], [https://www.ebi.ac.uk/pdbsum/4jgs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jgs ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/D0UFA8_9GAMR D0UFA8_9GAMR] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Membrane fusion is a key step in the life cycle of all envelope viruses, but this process is energetically unfavorable; the transmembrane fusion subunit (TM) of the virion-attached glycoprotein actively catalyzes the membrane merger process. Retroviral glycoproteins are the prototypical system to study pH-independent viral entry. In this study, we determined crystal structures of extramembrane regions of the TMs from Mason-Pfizer monkey virus (MPMV) and xenotropic murine leukemia virus-related virus (XMRV) at 1.7-A and 2.2-A resolution, respectively. The structures are comprised of a trimer of hairpins that is characteristic of class I viral fusion proteins and now completes a structural library of retroviral fusion proteins. Our results allowed us to identify a series of intra- and interchain electrostatic interactions in the heptad repeat and chain reversal regions. Mutagenesis reveals that charge-neutralizing salt bridge mutations significantly destabilize the postfusion six-helix bundle and abrogate retroviral infection, demonstrating that electrostatic stapling of the fusion subunit is essential for viral entry. Our data indicate that salt bridges are a major stabilizing force on the MPMV and XMRV retroviral TMs and likely provide the key energetics for viral and host membrane fusion. | ||
| - | + | Crystal structures of Beta- and gammaretrovirus fusion proteins reveal a role for electrostatic stapling in viral entry.,Aydin H, Cook JD, Lee JE J Virol. 2014 Jan;88(1):143-53. doi: 10.1128/JVI.02023-13. Epub 2013 Oct 16. PMID:24131724<ref>PMID:24131724</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4jgs" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Aydin H]] | ||
| + | [[Category: Cook JD]] | ||
| + | [[Category: Lee JE]] | ||
Current revision
Crystal structure of the xmrv tm retroviral fusion core
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