9krq: Difference between revisions
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==Crystal structure of ZXC21 RBD== | |||
<StructureSection load='9krq' size='340' side='right'caption='[[9krq]], [[Resolution|resolution]] 3.08Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9krq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bat_coronavirus Bat coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9KRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9KRQ 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]] 3.08Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=9krq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9krq OCA], [https://pdbe.org/9krq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9krq RCSB], [https://www.ebi.ac.uk/pdbsum/9krq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9krq ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A8A0R1U2_9NIDO A0A8A0R1U2_9NIDO] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bat coronaviruses ZXC21 and ZC45 were discovered before the COVID-19 outbreak and share approximately 86% genome homology with SARS-CoV-2. Earlier studies indicated that ZXC21 and ZC45 may be involved in the emergence of SARS-CoV-2. However, the cell invasion mechanisms of ZXC21 and ZC45 remain unclear. Here, we determined the crystal structure of the ZXC21 receptor-binding domain (RBD) and found that the core structure shared high similarity with SARS-CoV-2, MERS-CoV, human coronavirus (HCoV)-HKU1, SARS-CoV, and HCoV-OC43 RBDs, whereas the receptor-binding motifs (RBMs) differ. We demonstrated that the ZXC21 RBD had no interaction with the human coronavirus receptors angiotensin-converting enzyme 2 (ACE2), dipeptidylpeptidase 4 (DPP4), aminopeptidase N (APN), or transmembrane serine protease 2 (TMPRSS2) by surface plasmon resonance (SPR). Moreover, the P5S-3B11 Fab can bind to the ZXC21 RBD, indicating that this SARS-CoV-2 core-targeting antibody may retain neutralizing activity toward the ZXC21 coronavirus. Our results revealed the bat coronavirus ZXC21 RBD structure, which may provide further insights into the evolution of SARS-CoV-2 and the other human beta-coronaviruses. | |||
Structural insights into the receptor-binding domain of bat coronavirus ZXC21.,Wang C, Nan X, Deng Y, Fan S, Li X, Lan J Structure. 2025 Apr 23:S0969-2126(25)00138-8. doi: 10.1016/j.str.2025.04.004. PMID:40306273<ref>PMID:40306273</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 9krq" style="background-color:#fffaf0;"></div> | ||
[[Category: Lan | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bat coronavirus]] | |||
[[Category: Large Structures]] | |||
[[Category: Lan J]] | |||
[[Category: Wang CH]] | |||
