Structure.
Publisher:
Current Biology,. Cambridge, Mass. : Cell Press (2000)
Frequency: Monthly
Country: United States
Language: English
Start Year:1993 -
Identifiers
| ISSN: | 0969-2126 (Print) 1878-4186 (Electronic) 0969-2126 (Linking) |
| NLM ID: | 101087697 |
| (OCoLC): | 28867361 |
| Coden: | STRUE6 |
| LCCN: | 95645738 |
| Classification: | W1 ST81TM |
Structural insights into the binding of SARS-CoV-2, SARS-CoV, and hCoV-NL63 spike receptor-binding domain to horse ACE2. Severe acute respiratory syndrome coronavirus (SARS-CoV), SARS-CoV-2, and human coronavirus (hCoV)-NL63 utilize ACE2 as the functional receptor for cell entry, which leads to zoonotic infection. Horses (Equus caballus) attracted our attention because the spike protein receptor-binding domains (RBDs) of SARS-CoV-2 and SARS-CoV-2-related coronaviruses bind equine ACE2 (eACE2) with high affinity. Here we show that eACE2 binds the RBDs of these three coronaviruses and also SARS-CoV-2 variants but with lower affinities compared with human ACE2 (hACE2). Structural analysis and mutation assays indica...
The crystal structure of the Venezuelan equine encephalitis alphavirus nsP2 protease. Alphavirus replication and propagation is dependent on the protease activity of the viral nsP2 protein, which cleaves the nsP1234 polyprotein replication complex into functional components. Thus, nsP2 is an attractive target for drug discovery efforts to combat highly pathogenic alphaviruses. Unfortunately, antiviral development has been hampered by a lack of structural information for the nsP2 protease. Here, we report the crystal structure of the nsP2 protease (nsP2pro) from Venezuelan equine encephalitis alphavirus determined at 2.45 A resolution. The protease structure consists of two dist...