5tp3: Difference between revisions
New page: '''Unreleased structure''' The entry 5tp3 is ON HOLD Authors: Description: Category: Unreleased Structures |
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The | ==Crystal structure of the RSV-neutralizing single-domain antibody F-VHH-4== | ||
<StructureSection load='5tp3' size='340' side='right'caption='[[5tp3]], [[Resolution|resolution]] 1.87Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5tp3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lama_glama Lama glama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TP3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TP3 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.874Å</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=5tp3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tp3 OCA], [https://pdbe.org/5tp3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tp3 RCSB], [https://www.ebi.ac.uk/pdbsum/5tp3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tp3 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Human respiratory syncytial virus (RSV) is the main cause of lower respiratory tract infections in young children. The RSV fusion protein (F) is highly conserved and is the only viral membrane protein that is essential for infection. The prefusion conformation of RSV F is considered the most relevant target for antiviral strategies because it is the fusion-competent form of the protein and the primary target of neutralizing activity present in human serum. Here, we describe two llama-derived single-domain antibodies (VHHs) that have potent RSV-neutralizing activity and bind selectively to prefusion RSV F with picomolar affinity. Crystal structures of these VHHs in complex with prefusion F show that they recognize a conserved cavity formed by two F protomers. In addition, the VHHs prevent RSV replication and lung infiltration of inflammatory monocytes and T cells in RSV-challenged mice. These prefusion F-specific VHHs represent promising antiviral agents against RSV. | |||
Potent single-domain antibodies that arrest respiratory syncytial virus fusion protein in its prefusion state.,Rossey I, Gilman MS, Kabeche SC, Sedeyn K, Wrapp D, Kanekiyo M, Chen M, Mas V, Spitaels J, Melero JA, Graham BS, Schepens B, McLellan JS, Saelens X Nat Commun. 2017 Feb 13;8:14158. doi: 10.1038/ncomms14158. PMID:28194013<ref>PMID:28194013</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5tp3" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Antibody 3D structures|Antibody 3D structures]] | |||
*[[3D structures of non-human antibody|3D structures of non-human antibody]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Lama glama]] | |||
[[Category: Large Structures]] | |||
[[Category: Gilman MSA]] | |||
[[Category: McLellan JS]] | |||
[[Category: Wrapp D]] | |||
Latest revision as of 16:07, 4 October 2023
Crystal structure of the RSV-neutralizing single-domain antibody F-VHH-4Crystal structure of the RSV-neutralizing single-domain antibody F-VHH-4
Structural highlights
Publication Abstract from PubMedHuman respiratory syncytial virus (RSV) is the main cause of lower respiratory tract infections in young children. The RSV fusion protein (F) is highly conserved and is the only viral membrane protein that is essential for infection. The prefusion conformation of RSV F is considered the most relevant target for antiviral strategies because it is the fusion-competent form of the protein and the primary target of neutralizing activity present in human serum. Here, we describe two llama-derived single-domain antibodies (VHHs) that have potent RSV-neutralizing activity and bind selectively to prefusion RSV F with picomolar affinity. Crystal structures of these VHHs in complex with prefusion F show that they recognize a conserved cavity formed by two F protomers. In addition, the VHHs prevent RSV replication and lung infiltration of inflammatory monocytes and T cells in RSV-challenged mice. These prefusion F-specific VHHs represent promising antiviral agents against RSV. Potent single-domain antibodies that arrest respiratory syncytial virus fusion protein in its prefusion state.,Rossey I, Gilman MS, Kabeche SC, Sedeyn K, Wrapp D, Kanekiyo M, Chen M, Mas V, Spitaels J, Melero JA, Graham BS, Schepens B, McLellan JS, Saelens X Nat Commun. 2017 Feb 13;8:14158. doi: 10.1038/ncomms14158. PMID:28194013[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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