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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=7xaz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xaz OCA], [https://pdbe.org/7xaz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xaz RCSB], [https://www.ebi.ac.uk/pdbsum/7xaz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xaz 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=7xaz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xaz OCA], [https://pdbe.org/7xaz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xaz RCSB], [https://www.ebi.ac.uk/pdbsum/7xaz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xaz ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
The currently circulating Omicron sub-variants are the SARS-CoV-2 strains with the highest number of known mutations. Herein, we found that human angiotensin-converting enzyme 2 (hACE2) binding affinity to the receptor-binding domains (RBDs) of the four early Omicron sub-variants (BA.1, BA.1.1, BA.2, and BA.3) follows the order BA.1.1 > BA.2 > BA.3 approximately BA.1. The complex structures of hACE2 with RBDs of BA.1.1, BA.2, and BA.3 reveal that the higher hACE2 binding affinity of BA.2 than BA.1 is related to the absence of the G496S mutation in BA.2. The R346K mutation in BA.1.1 majorly affects the interaction network in the BA.1.1 RBD/hACE2 interface through long-range alterations and contributes to the higher hACE2 affinity of the BA.1.1 RBD than the BA.1 RBD. These results reveal the structural basis for the distinct hACE2 binding patterns among BA.1.1, BA.2, and BA.3 RBDs. | The currently circulating Omicron sub-variants are the SARS-CoV-2 strains with the highest number of known mutations. Herein, we found that human angiotensin-converting enzyme 2 (hACE2) binding affinity to the receptor-binding domains (RBDs) of the four early Omicron sub-variants (BA.1, BA.1.1, BA.2, and BA.3) follows the order BA.1.1 > BA.2 > BA.3 approximately BA.1. The complex structures of hACE2 with RBDs of BA.1.1, BA.2, and BA.3 reveal that the higher hACE2 binding affinity of BA.2 than BA.1 is related to the absence of the G496S mutation in BA.2. The R346K mutation in BA.1.1 majorly affects the interaction network in the BA.1.1 RBD/hACE2 interface through long-range alterations and contributes to the higher hACE2 affinity of the BA.1.1 RBD than the BA.1 RBD. These results reveal the structural basis for the distinct hACE2 binding patterns among BA.1.1, BA.2, and BA.3 RBDs. | ||
Structural basis of human ACE2 higher binding affinity to currently circulating Omicron SARS-CoV-2 sub-variants BA.2 and BA.1.1.,Li L, Liao H, Meng Y, Li W, Han P, Liu K, Wang Q, Li D, Zhang Y, Wang L, Fan Z, Zhang Y, Wang Q, Zhao X, Sun Y, Huang N, Qi J, Gao GF Cell. 2022 Aug 4;185(16):2952-2960.e10. doi: 10.1016/j.cell.2022.06.023. Epub, 2022 Jun 16. PMID:35809570<ref>PMID:35809570</ref> | Structural basis of human ACE2 higher binding affinity to currently circulating Omicron SARS-CoV-2 sub-variants BA.2 and BA.1.1.,Li L, Liao H, Meng Y, Li W, Han P, Liu K, Wang Q, Li D, Zhang Y, Wang L, Fan Z, Zhang Y, Wang Q, Zhao X, Sun Y, Huang N, Qi J, Gao GF Cell. 2022 Aug 4;185(16):2952-2960.e10. doi: 10.1016/j.cell.2022.06.023. Epub , 2022 Jun 16. PMID:35809570<ref>PMID:35809570</ref> | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
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==See Also== | ==See Also== | ||
*[[Angiotensin-Converting Enzyme 3D structures|Angiotensin-Converting Enzyme 3D structures]] | *[[Angiotensin-Converting Enzyme 3D structures|Angiotensin-Converting Enzyme 3D structures]] | ||
*[[Spike protein 3D structures|Spike protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 12:20, 17 October 2024
Crystal structure of Omicron BA.1.1 RBD complexed with hACE2Crystal structure of Omicron BA.1.1 RBD complexed with hACE2
Structural highlights
Publication Abstract from PubMedThe currently circulating Omicron sub-variants are the SARS-CoV-2 strains with the highest number of known mutations. Herein, we found that human angiotensin-converting enzyme 2 (hACE2) binding affinity to the receptor-binding domains (RBDs) of the four early Omicron sub-variants (BA.1, BA.1.1, BA.2, and BA.3) follows the order BA.1.1 > BA.2 > BA.3 approximately BA.1. The complex structures of hACE2 with RBDs of BA.1.1, BA.2, and BA.3 reveal that the higher hACE2 binding affinity of BA.2 than BA.1 is related to the absence of the G496S mutation in BA.2. The R346K mutation in BA.1.1 majorly affects the interaction network in the BA.1.1 RBD/hACE2 interface through long-range alterations and contributes to the higher hACE2 affinity of the BA.1.1 RBD than the BA.1 RBD. These results reveal the structural basis for the distinct hACE2 binding patterns among BA.1.1, BA.2, and BA.3 RBDs. Structural basis of human ACE2 higher binding affinity to currently circulating Omicron SARS-CoV-2 sub-variants BA.2 and BA.1.1.,Li L, Liao H, Meng Y, Li W, Han P, Liu K, Wang Q, Li D, Zhang Y, Wang L, Fan Z, Zhang Y, Wang Q, Zhao X, Sun Y, Huang N, Qi J, Gao GF Cell. 2022 Aug 4;185(16):2952-2960.e10. doi: 10.1016/j.cell.2022.06.023. Epub , 2022 Jun 16. PMID:35809570[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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