This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4d6w

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 17:32, 18 January 2017

Crystal Structure of the low pH conformation of Chandipura Virus glycoprotein G ectodomain

Structural highlights

4d6w is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GLYCO_CHAV] Attaches the virus to host cellular receptor, inducing endocytosis of the virion. In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and cell membrane (By similarity).

Publication Abstract from PubMed

Chandipura virus (CHAV), a member of the vesiculovirus genus, is an emerging human pathogen. As for other rhabdoviruses, CHAV entry into susceptible cells is mediated by its single envelope glycoprotein G which is both involved in receptor recognition and fusion of viral and cellular membranes. Here, we have characterized the fusion properties of CHAV-G. As for vesicular stomatitis virus (VSV, the prototype of the genus) G, fusion is triggered at low pH below 6.5. We have also analyzed the biochemical properties of a soluble form of CHAV-G ectodomain (CHAV-Gth, generated by thermolysin limited-proteolysis of recombinant VSV particles in which the G gene was replaced by that of CHAV). The overall behavior of CHAV-Gth is similar to that previously reported for VSV-Gth. Particularly, CHAV-Gth pre-fusion trimer is not stable in solution and low-pH-induced membrane association of CHAV-Gth is reversible. Furthermore, CHAV-Gth was crystallized in its low pH post-fusion conformation and its structure was determined at 3.6A resolution. An overall comparison of this structure with the previously reported VSV-Gth post-fusion conformation, shows a high structural similarity as expected from the comparison of primary structure. Among the three domains of G, the pleckstrin homology domain (PHD) appears to be the most divergent and the largest differences are confined to the secondary structure of the major antigenic site of rhabdoviruses. Finally, local differences indicate that CHAV has evolved alternate structural solutions in hinge regions between PH and fusion domains but also distinct pH sensitive switches. Globally the comparison between the post fusion conformation of CHAV and VSV-G highlights several features essential for the protein's function. It also reveals the remarkable plasticity of G in terms of local structures.

Structure of the Low pH Conformation of Chandipura Virus G Reveals Important Features in the Evolution of the Vesiculovirus Glycoprotein.,Baquero E, Albertini AA, Raux H, Buonocore L, Rose JK, Bressanelli S, Gaudin Y PLoS Pathog. 2015 Mar 24;11(3):e1004756. doi: 10.1371/journal.ppat.1004756., eCollection 2015 Mar. PMID:25803715^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Baquero E, Albertini AA, Raux H, Buonocore L, Rose JK, Bressanelli S, Gaudin Y. Structure of the Low pH Conformation of Chandipura Virus G Reveals Important Features in the Evolution of the Vesiculovirus Glycoprotein. PLoS Pathog. 2015 Mar 24;11(3):e1004756. doi: 10.1371/journal.ppat.1004756., eCollection 2015 Mar. PMID:25803715 doi:http://dx.doi.org/10.1371/journal.ppat.1004756

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4d6w"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of the low pH conformation of Chandipura Virus glycoprotein G ectodomain==
 <StructureSection load='4d6w' size='340' side='right' caption='[[4d6w]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[4d6w]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D6W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D6W FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</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=4d6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d6w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4d6w RCSB], [http://www.ebi.ac.uk/pdbsum/4d6w PDBsum]</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=4d6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d6w OCA], [http://pdbe.org/4d6w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d6w RCSB], [http://www.ebi.ac.uk/pdbsum/4d6w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d6w ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4d6w" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4d6w

From Proteopedia

Revision as of 17:32, 18 January 2017

Crystal Structure of the low pH conformation of Chandipura Virus glycoprotein G ectodomain

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox