7a59

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Current revision (10:49, 23 October 2024) (edit) (undo)
 
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<StructureSection load='7a59' size='340' side='right'caption='[[7a59]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='7a59' size='340' side='right'caption='[[7a59]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7a59]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7A59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A59 FirstGlance]. <br>
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7A59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A59 FirstGlance]. <br>
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</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.197&#8491;</td></tr>
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<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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=7a59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a59 OCA], [https://pdbe.org/7a59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a59 RCSB], [https://www.ebi.ac.uk/pdbsum/7a59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a59 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=7a59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a59 OCA], [https://pdbe.org/7a59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a59 RCSB], [https://www.ebi.ac.uk/pdbsum/7a59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a59 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
 
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[[https://www.uniprot.org/uniprot/GP_CCHFI GP_CCHFI]] Glycoprotein C and glycoprotein N interact with each other and are present at the surface of the virion. They are able to attach the virion to host cell receptors. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Also promotes fusion of viral membrane with host endosomal membrane after endocytosis of the virion (By similarity).<ref>PMID:19088291</ref>
 
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Crimean-Congo hemorrhagic fever virus (CCHFV) is the most widespread tick-borne zoonotic virus, with a 30% case fatality rate in humans. Structural information is lacking in regard to the CCHFV membrane fusion glycoprotein Gc-the main target of the host neutralizing antibody response-as well as antibody-mediated neutralization mechanisms. We describe the structure of prefusion Gc bound to the antigen-binding fragments (Fabs) of two neutralizing antibodies that display synergy when combined, as well as the structure of trimeric, postfusion Gc. The structures show the two Fabs acting in concert to block membrane fusion, with one targeting the fusion loops and the other blocking Gc trimer formation. The structures also revealed the neutralization mechanism of previously reported antibodies against CCHFV, providing the molecular underpinnings essential for developing CCHFV-specific medical countermeasures for epidemic preparedness.
 
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Structural basis of synergistic neutralization of Crimean-Congo hemorrhagic fever virus by human antibodies.,Mishra AK, Hellert J, Freitas N, Guardado-Calvo P, Haouz A, Fels JM, Maurer DP, Abelson DM, Bornholdt ZA, Walker LM, Chandran K, Cosset FL, McLellan JS, Rey FA Science. 2022 Jan 7;375(6576):104-109. doi: 10.1126/science.abl6502. Epub 2021, Nov 18. PMID:34793197<ref>PMID:34793197</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 7a59" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Guardado-Calvo, P]]
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[[Category: Guardado-Calvo P]]
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[[Category: Hellert, J]]
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[[Category: Hellert J]]
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[[Category: Rey, F A]]
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[[Category: Rey FA]]
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[[Category: Class ii membrane fusion protein]]
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[[Category: Viral protein]]
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[[Category: Virus entry]]
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Current revision

Crimean-Congo Hemorrhagic Fever Virus Envelope Glycoprotein Gc W1191H/W1197A/W1199A Mutant in Postfusion Conformation (Orthorhombic Crystal Form)

PDB ID 7a59

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