7d30: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7d30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d30 OCA], [https://pdbe.org/7d30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d30 RCSB], [https://www.ebi.ac.uk/pdbsum/7d30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d30 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=7d30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d30 OCA], [https://pdbe.org/7d30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d30 RCSB], [https://www.ebi.ac.uk/pdbsum/7d30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d30 ProSAT]</span></td></tr> | ||
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<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Antibody 3D structures|Antibody 3D structures]] | *[[Antibody 3D structures|Antibody 3D structures]] | ||
*[[Spike protein 3D structures|Spike protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 12:23, 9 October 2024
Structure of sybody MR17-SR31 fusion in complex with the SARS-CoV-2 S Receptor Binding domain (RBD)Structure of sybody MR17-SR31 fusion in complex with the SARS-CoV-2 S Receptor Binding domain (RBD)
Structural highlights
Publication Abstract from PubMedA key step to the SARS-CoV-2 infection is the attachment of its Spike receptor-binding domain (S RBD) to the host receptor ACE2. Considerable research has been devoted to the development of neutralizing antibodies, including llama-derived single-chain nanobodies, to target the receptor-binding motif (RBM) and to block ACE2-RBD binding. Simple and effective strategies to increase potency are desirable for such studies when antibodies are only modestly effective. Here, we identify and characterize a high-affinity synthetic nanobody (sybody, SR31) as a fusion partner to improve the potency of RBM-antibodies. Crystallographic studies reveal that SR31 binds to RBD at a conserved and 'greasy' site distal to RBM. Although SR31 distorts RBD at the interface, it does not perturb the RBM conformation, hence displaying no neutralizing activities itself. However, fusing SR31 to two modestly neutralizing sybodies dramatically increases their affinity for RBD and neutralization activity against SARS-CoV-2 pseudovirus. Our work presents a tool protein and an efficient strategy to improve nanobody potency. A high-affinity RBD-targeting nanobody improves fusion partner's potency against SARS-CoV-2.,Yao H, Cai H, Li T, Zhou B, Qin W, Lavillette D, Li D PLoS Pathog. 2021 Mar 3;17(3):e1009328. doi: 10.1371/journal.ppat.1009328. , eCollection 2021 Mar. PMID:33657135[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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