7wsf: Difference between revisions
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==Cryo-EM structure of SARS-CoV spike receptor-binding domain in complex with minke whale ACE2== | |||
<StructureSection load='7wsf' size='340' side='right'caption='[[7wsf]], [[Resolution|resolution]] 2.87Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7wsf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mammalia Mammalia] and [https://en.wikipedia.org/wiki/Severe_acute_respiratory_syndrome_coronavirus Severe acute respiratory syndrome coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WSF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WSF FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7wsf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wsf OCA], [https://pdbe.org/7wsf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wsf RCSB], [https://www.ebi.ac.uk/pdbsum/7wsf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wsf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A452CBT6_BALAS A0A452CBT6_BALAS] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has an extremely broad host range that includes hippopotami, which are phylogenetically closely related to whales. The cellular ACE2 receptor is one of the key determinants of the host range. Here, we found that ACE2s from several marine mammals and hippopotami could efficiently bind to the receptor-binding domain (RBD) of both SARS-CoV and SARS-CoV-2 and facilitate the transduction of SARS-CoV and SARS-CoV-2 pseudoviruses into ACE2-expressing cells. We further resolved the cryo-electron microscopy complex structures of the minke whale ACE2 and sea lion ACE2, respectively, bound to the RBDs, revealing that they have similar binding modes to human ACE2 when it comes to the SARS-CoV-2 RBD and SARS-CoV RBD. Our results indicate that marine mammals could potentially be new victims or virus carriers of SARS-CoV-2, which deserves further careful investigation and study. It will provide an early warning for the prospective monitoring of marine mammals. | |||
Cross-species recognition and molecular basis of SARS-CoV-2 and SARS-CoV binding to ACE2s of marine animals.,Li S, Yang R, Zhang D, Han P, Xu Z, Chen Q, Zhao R, Zhao X, Qu X, Zheng A, Wang L, Li L, Hu Y, Zhang R, Su C, Niu S, Zhang Y, Qi J, Liu K, Wang Q, Gao GF Natl Sci Rev. 2022 Jun 23;9(9):nwac122. doi: 10.1093/nsr/nwac122. eCollection, 2022 Sep. PMID:36187898<ref>PMID:36187898</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7wsf" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mammalia]] | |||
[[Category: Severe acute respiratory syndrome coronavirus]] | |||
[[Category: Han P]] | |||
[[Category: Li S]] | |||
[[Category: Qi J]] | |||
Latest revision as of 22:23, 19 October 2022
Cryo-EM structure of SARS-CoV spike receptor-binding domain in complex with minke whale ACE2Cryo-EM structure of SARS-CoV spike receptor-binding domain in complex with minke whale ACE2
Structural highlights
FunctionPublication Abstract from PubMedSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has an extremely broad host range that includes hippopotami, which are phylogenetically closely related to whales. The cellular ACE2 receptor is one of the key determinants of the host range. Here, we found that ACE2s from several marine mammals and hippopotami could efficiently bind to the receptor-binding domain (RBD) of both SARS-CoV and SARS-CoV-2 and facilitate the transduction of SARS-CoV and SARS-CoV-2 pseudoviruses into ACE2-expressing cells. We further resolved the cryo-electron microscopy complex structures of the minke whale ACE2 and sea lion ACE2, respectively, bound to the RBDs, revealing that they have similar binding modes to human ACE2 when it comes to the SARS-CoV-2 RBD and SARS-CoV RBD. Our results indicate that marine mammals could potentially be new victims or virus carriers of SARS-CoV-2, which deserves further careful investigation and study. It will provide an early warning for the prospective monitoring of marine mammals. Cross-species recognition and molecular basis of SARS-CoV-2 and SARS-CoV binding to ACE2s of marine animals.,Li S, Yang R, Zhang D, Han P, Xu Z, Chen Q, Zhao R, Zhao X, Qu X, Zheng A, Wang L, Li L, Hu Y, Zhang R, Su C, Niu S, Zhang Y, Qi J, Liu K, Wang Q, Gao GF Natl Sci Rev. 2022 Jun 23;9(9):nwac122. doi: 10.1093/nsr/nwac122. eCollection, 2022 Sep. PMID:36187898[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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