4jha: Difference between revisions
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==Crystal Structure of RSV-Neutralizing Human Antibody D25== | ==Crystal Structure of RSV-Neutralizing Human Antibody D25== | ||
<StructureSection load='4jha' size='340' side='right' caption='[[4jha]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='4jha' size='340' side='right'caption='[[4jha]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4jha]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4jha]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JHA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JHA FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4jha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jha OCA], [https://pdbe.org/4jha PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jha RCSB], [https://www.ebi.ac.uk/pdbsum/4jha PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jha ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Baxa | [[Category: Large Structures]] | ||
[[Category: Beaumont | [[Category: Baxa U]] | ||
[[Category: Chen | [[Category: Beaumont T]] | ||
[[Category: Du | [[Category: Chen M]] | ||
[[Category: Graepel | [[Category: Du X]] | ||
[[Category: Graham | [[Category: Graepel KW]] | ||
[[Category: Kumar | [[Category: Graham BS]] | ||
[[Category: Kwong | [[Category: Kumar A]] | ||
[[Category: Leung | [[Category: Kwong PD]] | ||
[[Category: Mclellan | [[Category: Leung S]] | ||
[[Category: Modjarrad | [[Category: Mclellan JS]] | ||
[[Category: Xia | [[Category: Modjarrad K]] | ||
[[Category: Yang | [[Category: Xia N]] | ||
[[Category: Yasuda | [[Category: Yang Y]] | ||
[[Category: Zhao | [[Category: Yasuda E]] | ||
[[Category: Zheng | [[Category: Zhao M]] | ||
[[Category: Zhou | [[Category: Zheng Z]] | ||
[[Category: Zhou T]] | |||
Latest revision as of 18:42, 20 September 2023
Crystal Structure of RSV-Neutralizing Human Antibody D25Crystal Structure of RSV-Neutralizing Human Antibody D25
Structural highlights
Publication Abstract from PubMedThe prefusion state of respiratory syncytial virus (RSV) fusion (F) glycoprotein is the target of most RSV-neutralizing activity in human sera, but its metastability has hindered characterization. To overcome this obstacle, we identified prefusion-specific antibodies that were substantially more potent than the prophylactic antibody palivizumab. The cocrystal structure for one of these antibodies, D25, in complex with the F glycoprotein revealed D25 to lock F in its prefusion state by binding to a quaternary epitope at the trimer apex. Electron microscopy showed that two other antibodies, AM22 and 5C4, also bound to the newly identified site of vulnerability, which we named antigenic site O. These studies should enable design of improved vaccine antigens and define new targets for passive prevention of RSV-induced disease. Structure of RSV fusion glycoprotein trimer bound to a prefusion-specific neutralizing antibody.,McLellan JS, Chen M, Leung S, Graepel KW, Du X, Yang Y, Zhou T, Baxa U, Yasuda E, Beaumont T, Kumar A, Modjarrad K, Zheng Z, Zhao M, Xia N, Kwong PD, Graham BS Science. 2013 May 31;340(6136):1113-7. doi: 10.1126/science.1234914. Epub 2013, Apr 25. PMID:23618766[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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