8aez

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:26, 17 October 2024) (edit) (undo)
 
Line 4: Line 4:
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[8aez]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Simian_foamy_virus Simian foamy virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AEZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AEZ FirstGlance]. <br>
<table><tr><td colspan='2'>[[8aez]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Simian_foamy_virus Simian foamy virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AEZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AEZ FirstGlance]. <br>
-
</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>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.574&#8491;</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'>[https://proteopedia.org/fgij/fg.htm?mol=8aez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8aez OCA], [https://pdbe.org/8aez PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8aez RCSB], [https://www.ebi.ac.uk/pdbsum/8aez PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8aez 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=8aez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8aez OCA], [https://pdbe.org/8aez PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8aez RCSB], [https://www.ebi.ac.uk/pdbsum/8aez PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8aez ProSAT]</span></td></tr>
</table>
</table>
-
== Function ==
+
<div style="background-color:#fffaf0;">
-
[https://www.uniprot.org/uniprot/K7YEW5_9RETR K7YEW5_9RETR] The leader peptide is a component of released, infectious virions and is required for particle budding.[ARBA:ARBA00002261] The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.[ARBA:ARBA00024648]
+
== Publication Abstract from PubMed ==
 +
The surface envelope glycoprotein (Env) of all retroviruses mediates virus binding to cells and fusion of the viral and cellular membranes. A structure-function relationship for the HIV Env that belongs to the Orthoretrovirus subfamily has been well established. Structural information is however largely missing for the Env of Foamy viruses (FVs), the second retroviral subfamily. In this work we present the X-ray structure of the receptor binding domain (RBD) of a simian FV Env at 2.57 A resolution, revealing two subdomains and an unprecedented fold. We have generated a model for the organization of the RBDs within the trimeric Env, which indicates that the upper subdomains form a cage-like structure at the apex of the Env, and identified residues K342, R343, R359 and R369 in the lower subdomain as key players for the interaction of the RBD and viral particles with heparan sulfate.
 +
 
 +
The crystal structure of a simian Foamy Virus receptor binding domain provides clues about entry into host cells.,Fernandez I, Dynesen LT, Coquin Y, Pederzoli R, Brun D, Haouz A, Gessain A, Rey FA, Buseyne F, Backovic M Nat Commun. 2023 Mar 6;14(1):1262. doi: 10.1038/s41467-023-36923-0. PMID:36878926<ref>PMID:36878926</ref>
 +
 
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 8aez" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

X-ray structure of the deglycosylated receptor binding domain of Env glycoprotein of Simian Foamy virus

PDB ID 8aez

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/8aez"
Personal tools