| Title |
Structural basis of human ACE2 higher binding affinity to currently circulating Omicron SARS-CoV-2 sub-variants BA.2 and BA.1.1 |
| Description |
we found that human angiotensin-converting enzyme 2 (hACE2) binding affinity to the re- ceptor-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 z 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. |
| Organism |
Homo sapiens |
| Data Type |
Other Type of Proteomic Data |
| Data Accessibility |
Controlled-access |
| BioProject |
PRJCA016203 |
| Release Date |
2024-12-31 |
| Submitter |
Li Jing (lijing@im.ac.cn) |
| Organization |
Institute of Microbiology, Chinese Academy of Sciences |
| Submission Date |
2023-05-05 |