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| | <StructureSection load='4gq9' size='340' side='right'caption='[[4gq9]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='4gq9' size='340' side='right'caption='[[4gq9]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4gq9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GQ9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GQ9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4gq9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GQ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GQ9 FirstGlance]. <br> |
| - | </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=4gq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gq9 OCA], [http://pdbe.org/4gq9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gq9 RCSB], [http://www.ebi.ac.uk/pdbsum/4gq9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gq9 ProSAT]</span></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]] 2.995Å</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=4gq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gq9 OCA], [https://pdbe.org/4gq9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gq9 RCSB], [https://www.ebi.ac.uk/pdbsum/4gq9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gq9 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | ==See Also== | | ==See Also== |
| | *[[Antibody 3D structures|Antibody 3D structures]] | | *[[Antibody 3D structures|Antibody 3D structures]] |
| | + | *[[Sandbox 20009|Sandbox 20009]] |
| | + | *[[3D structures of non-human antibody|3D structures of non-human antibody]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Mus musculus]] | | [[Category: Mus musculus]] |
| - | [[Category: Rossmann, M G]] | + | [[Category: Rossmann MG]] |
| - | [[Category: Sun, S]] | + | [[Category: Sun S]] |
| - | [[Category: Antibody]]
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| - | [[Category: Igg fold]]
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| - | [[Category: Viral protein]]
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| Structural highlights
Publication Abstract from PubMed
A 5.3 A resolution, cryo-electron microscopy (cryoEM) map of Chikungunya virus-like particles (VLPs) has been interpreted using the previously published crystal structure of the Chikungunya E1-E2 glycoprotein heterodimer. The heterodimer structure was divided into domains to obtain a good fit to the cryoEM density. Differences in the T = 4 quasi-equivalent heterodimer components show their adaptation to different environments. The spikes on the icosahedral 3-fold axes and those in general positions are significantly different, possibly representing different phases during initial generation of fusogenic E1 trimers. CryoEM maps of neutralizing Fab fragments complexed with VLPs have been interpreted using the crystal structures of the Fab fragments and the VLP structure. Based on these analyses the CHK-152 antibody was shown to stabilize the viral surface, hindering the exposure of the fusion-loop, likely neutralizing infection by blocking fusion. The CHK-9, m10 and m242 antibodies surround the receptor-attachment site, probably inhibiting infection by blocking cell attachment. DOI:http://dx.doi.org/10.7554/eLife.00435.001.
Structural analyses at pseudo atomic resolution of Chikungunya virus and antibodies show mechanisms of neutralization.,Sun S, Xiang Y, Akahata W, Holdaway H, Pal P, Zhang X, Diamond MS, Nabel GJ, Rossmann MG Elife. 2013;2:e00435. doi: 10.7554/eLife.00435. Epub 2013 Apr 2. PMID:23577234[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sun S, Xiang Y, Akahata W, Holdaway H, Pal P, Zhang X, Diamond MS, Nabel GJ, Rossmann MG. Structural analyses at pseudo atomic resolution of Chikungunya virus and antibodies show mechanisms of neutralization. Elife. 2013;2:e00435. doi: 10.7554/eLife.00435. Epub 2013 Apr 2. PMID:23577234 doi:10.7554/eLife.00435
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