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5ine

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Revision as of 14:02, 30 August 2023

Crystal structure of the prefusion glycoprotein of LCMV

Structural highlights

5ine is a 2 chain structure with sequence from Lymphocytic choriomeningitis mammarenavirus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.5Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GLYC_LYCVW The stable signal peptide (SSP) is cleaved and functions as a signal peptide. In addition, it is apparently retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of GP1 and GP2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion (By similarity). Glycoprotein G1 mediates virus attachment to host receptor alpha-dystroglycan DAG1. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis (By similarity). Glycoprotein G2 is a viral fusion protein. Membrane fusion is mediated by conformational changes induced upon acidification in the endosome (Potential).

Publication Abstract from PubMed

Arenaviruses exist worldwide and can cause hemorrhagic fever and neurologic disease. A single glycoprotein expressed on the viral surface mediates entry into target cells. This glycoprotein, termed GPC, contains a membrane-associated signal peptide, a receptor-binding subunit termed GP1 and a fusion-mediating subunit termed GP2. Although GPC is a critical target of antibodies and vaccines, the structure of the metastable GP1-GP2 prefusion complex has remained elusive for all arenaviruses. Here we describe the crystal structure of the fully glycosylated prefusion GP1-GP2 complex of the prototypic arenavirus LCMV at 3.5 A. This structure reveals the conformational changes that the arenavirus glycoprotein must undergo to cause fusion and illustrates the fusion regions and potential oligomeric states.

Crystal structure of the prefusion surface glycoprotein of the prototypic arenavirus LCMV.,Hastie KM, Igonet S, Sullivan BM, Legrand P, Zandonatti MA, Robinson JE, Garry RF, Rey FA, Oldstone MB, Saphire EO Nat Struct Mol Biol. 2016 Apr 25. doi: 10.1038/nsmb.3210. PMID:27111888^[1]

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

References

↑ Hastie KM, Igonet S, Sullivan BM, Legrand P, Zandonatti MA, Robinson JE, Garry RF, Rey FA, Oldstone MB, Saphire EO. Crystal structure of the prefusion surface glycoprotein of the prototypic arenavirus LCMV. Nat Struct Mol Biol. 2016 Apr 25. doi: 10.1038/nsmb.3210. PMID:27111888 doi:http://dx.doi.org/10.1038/nsmb.3210

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/5ine"

Categories: Large Structures | Lymphocytic choriomeningitis mammarenavirus | Hastie KM | Saphire EO

@@ Line 3: / Line 3: @@
 <StructureSection load='5ine' size='340' side='right'caption='[[5ine]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5ine]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lcmv Lcmv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5INE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5INE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5ine]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lymphocytic_choriomeningitis_mammarenavirus Lymphocytic choriomeningitis mammarenavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5INE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5INE FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gp-C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11623 LCMV])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=5ine FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ine OCA], [http://pdbe.org/5ine PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ine RCSB], [http://www.ebi.ac.uk/pdbsum/5ine PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ine ProSAT]</span></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=5ine FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ine OCA], [https://pdbe.org/5ine PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ine RCSB], [https://www.ebi.ac.uk/pdbsum/5ine PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ine ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/GLYC_LYCVW GLYC_LYCVW] The stable signal peptide (SSP) is cleaved and functions as a signal peptide. In addition, it is apparently retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of GP1 and GP2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion (By similarity).  Glycoprotein G1 mediates virus attachment to host receptor alpha-dystroglycan DAG1. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis (By similarity).  Glycoprotein G2 is a viral fusion protein. Membrane fusion is mediated by conformational changes induced upon acidification in the endosome (Potential).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 24: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Lcmv]]
+[[Category: Lymphocytic choriomeningitis mammarenavirus]]
-[[Category: Hastie, K M]]
+[[Category: Hastie KM]]
-[[Category: Saphire, E O]]
+[[Category: Saphire EO]]
-[[Category: Arenavirus]]
-[[Category: Glycoprotein]]
-[[Category: Pre-fusion]]
-[[Category: Viral protein]]

5ine

From Proteopedia

Revision as of 14:02, 30 August 2023

Crystal structure of the prefusion glycoprotein of LCMV

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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