7drv: Difference between revisions
New page: '''Unreleased structure''' The entry 7drv is ON HOLD Authors: Description: Category: Unreleased Structures |
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==Structural basis of SARS-CoV-2-closely-related bat coronavirus RaTG13 to hACE2== | |||
<StructureSection load='7drv' size='340' side='right'caption='[[7drv]], [[Resolution|resolution]] 3.09Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7drv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bat_coronavirus_RaTG13 Bat coronavirus RaTG13] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DRV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DRV 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]] 3.09Å</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>, <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=7drv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7drv OCA], [https://pdbe.org/7drv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7drv RCSB], [https://www.ebi.ac.uk/pdbsum/7drv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7drv ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ACE2_HUMAN ACE2_HUMAN] Carboxypeptidase which converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator. Also able to hydrolyze apelin-13 and dynorphin-13 with high efficiency. May be an important regulator of heart function. In case of human coronaviruses SARS and HCoV-NL63 infections, serve as functional receptor for the spike glycoprotein of both coronaviruses.<ref>PMID:10969042</ref> <ref>PMID:10924499</ref> <ref>PMID:14647384</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has been spreading worldwide, causing a global pandemic. Bat-origin RaTG13 is currently the most phylogenetically related virus. Here we obtained the complex structure of the RaTG13 receptor binding domain (RBD) with human ACE2 (hACE2) and evaluated binding of RaTG13 RBD to 24 additional ACE2 orthologs. By substituting residues in the RaTG13 RBD with their counterparts in the SARS-CoV-2 RBD, we found that residue 501, the major position found in variants of concern (VOCs) 501Y.V1/V2/V3, plays a key role in determining the potential host range of RaTG13. We also found that SARS-CoV-2 could induce strong cross-reactive antibodies to RaTG13 and identified a SARS-CoV-2 monoclonal antibody (mAb), CB6, that could cross-neutralize RaTG13 pseudovirus. These results elucidate the receptor binding and host adaption mechanisms of RaTG13 and emphasize the importance of continuous surveillance of coronaviruses (CoVs) carried by animal reservoirs to prevent another spillover of CoVs. | |||
Binding and molecular basis of the bat coronavirus RaTG13 virus to ACE2 in humans and other species.,Liu K, Pan X, Li L, Yu F, Zheng A, Du P, Han P, Meng Y, Zhang Y, Wu L, Chen Q, Song C, Jia Y, Niu S, Lu D, Qiao C, Chen Z, Ma D, Ma X, Tan S, Zhao X, Qi J, Gao GF, Wang Q Cell. 2021 Jun 24;184(13):3438-3451.e10. doi: 10.1016/j.cell.2021.05.031. Epub , 2021 May 24. PMID:34139177<ref>PMID:34139177</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7drv" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Angiotensin-Converting Enzyme 3D structures|Angiotensin-Converting Enzyme 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bat coronavirus RaTG13]] | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Chen Q]] | |||
[[Category: Feng Y]] | |||
[[Category: Gao GF]] | |||
[[Category: Jia YF]] | |||
[[Category: Li LJ]] | |||
[[Category: Liu KF]] | |||
[[Category: Ma DL]] | |||
[[Category: Ma XP]] | |||
[[Category: Meng YM]] | |||
[[Category: Niu S]] | |||
[[Category: Pan XQ]] | |||
[[Category: Qi JX]] | |||
[[Category: Qiao CP]] | |||
[[Category: Song CL]] | |||
[[Category: Tan SG]] | |||
[[Category: Wang QH]] | |||
[[Category: Wu LL]] | |||
[[Category: Zhang YF]] | |||
[[Category: Zhao X]] | |||
[[Category: Zheng AQ]] | |||
Latest revision as of 19:38, 29 November 2023
Structural highlights
FunctionACE2_HUMAN Carboxypeptidase which converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator. Also able to hydrolyze apelin-13 and dynorphin-13 with high efficiency. May be an important regulator of heart function. In case of human coronaviruses SARS and HCoV-NL63 infections, serve as functional receptor for the spike glycoprotein of both coronaviruses.[1] [2] [3] Publication Abstract from PubMedSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has been spreading worldwide, causing a global pandemic. Bat-origin RaTG13 is currently the most phylogenetically related virus. Here we obtained the complex structure of the RaTG13 receptor binding domain (RBD) with human ACE2 (hACE2) and evaluated binding of RaTG13 RBD to 24 additional ACE2 orthologs. By substituting residues in the RaTG13 RBD with their counterparts in the SARS-CoV-2 RBD, we found that residue 501, the major position found in variants of concern (VOCs) 501Y.V1/V2/V3, plays a key role in determining the potential host range of RaTG13. We also found that SARS-CoV-2 could induce strong cross-reactive antibodies to RaTG13 and identified a SARS-CoV-2 monoclonal antibody (mAb), CB6, that could cross-neutralize RaTG13 pseudovirus. These results elucidate the receptor binding and host adaption mechanisms of RaTG13 and emphasize the importance of continuous surveillance of coronaviruses (CoVs) carried by animal reservoirs to prevent another spillover of CoVs. Binding and molecular basis of the bat coronavirus RaTG13 virus to ACE2 in humans and other species.,Liu K, Pan X, Li L, Yu F, Zheng A, Du P, Han P, Meng Y, Zhang Y, Wu L, Chen Q, Song C, Jia Y, Niu S, Lu D, Qiao C, Chen Z, Ma D, Ma X, Tan S, Zhao X, Qi J, Gao GF, Wang Q Cell. 2021 Jun 24;184(13):3438-3451.e10. doi: 10.1016/j.cell.2021.05.031. Epub , 2021 May 24. PMID:34139177[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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