2xz3: Difference between revisions
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<StructureSection load='2xz3' size='340' side='right' caption='[[2xz3]], [[Resolution|resolution]] 1.95Å' scene=''> | <StructureSection load='2xz3' size='340' side='right' caption='[[2xz3]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2xz3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XZ3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XZ3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2xz3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Blv Blv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XZ3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XZ3 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xz3 OCA], [http://pdbe.org/2xz3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xz3 RCSB], [http://www.ebi.ac.uk/pdbsum/2xz3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xz3 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xz3 OCA], [http://pdbe.org/2xz3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xz3 RCSB], [http://www.ebi.ac.uk/pdbsum/2xz3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xz3 ProSAT]</span></td></tr> | ||
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</div> | </div> | ||
<div class="pdbe-citations 2xz3" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2xz3" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Blv]] | |||
[[Category: Aalten, D M.F van]] | [[Category: Aalten, D M.F van]] | ||
[[Category: Brighty, D W]] | [[Category: Brighty, D W]] | ||
Revision as of 17:34, 15 November 2017
BLV TM hairpinBLV TM hairpin
Structural highlights
Publication Abstract from PubMedRefolding of viral class-1 membrane fusion proteins from a native state to a trimer-of-hairpins structure promotes entry of viruses into cells. Here we present the structure of the bovine leukaemia virus transmembrane glycoprotein (TM) and identify a group of asparagine residues at the membrane-distal end of the trimer-of-hairpins that is strikingly conserved among divergent viruses. These asparagines are not essential for surface display of pre-fusogenic envelope. Instead, substitution of these residues dramatically disrupts membrane fusion. Our data indicate that, through electrostatic interactions with a chloride ion, the asparagine residues promote assembly and profoundly stabilize the fusion-active structures that are required for viral envelope-mediated membrane fusion. Moreover, the BLV TM structure also reveals a charge-surrounded hydrophobic pocket on the central coiled coil and interactions with basic residues that cluster around this pocket are critical to membrane fusion and form a target for peptide inhibitors of envelope function. Charge-surrounded pockets and electrostatic interactions with small ions are common among class-1 fusion proteins, suggesting that small molecules that specifically target such motifs should prevent assembly of the trimer-of-hairpins and be of value as therapeutic inhibitors of viral entry. Charge-surrounded pockets and electrostatic interactions with small ions modulate the activity of retroviral fusion proteins.,Lamb D, Schuttelkopf AW, van Aalten DM, Brighty DW PLoS Pathog. 2011 Feb 3;7(2):e1001268. PMID:21304939[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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