Pub. Date : 2020 Aug 13
PMID : 32521159
11 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | Here, we used molecular dynamics simulations and free energy perturbation methods to study the inhibition mechanism of remdesivir to its target SARS-CoV-2 virus RNA-dependent RNA polymerase (RdRp). | remdesivir | ORF1a polyprotein;ORF1ab polyprotein | Severe acute respiratory syndrome coronavirus 2 |
2 | We then built a putative preinsertion binding structure by aligning the remdesivir + RdRp complex to the ATP bound poliovirus RdRp without the RNA template. | remdesivir | ORF1a polyprotein;ORF1ab polyprotein | Severe acute respiratory syndrome coronavirus 2 |
3 | We then built a putative preinsertion binding structure by aligning the remdesivir + RdRp complex to the ATP bound poliovirus RdRp without the RNA template. | remdesivir | ORF1a polyprotein;ORF1ab polyprotein | Severe acute respiratory syndrome coronavirus 2 |
4 | We then built a putative preinsertion binding structure by aligning the remdesivir + RdRp complex to the ATP bound poliovirus RdRp without the RNA template. | Adenosine Triphosphate | ORF1a polyprotein;ORF1ab polyprotein | Severe acute respiratory syndrome coronavirus 2 |
5 | The resulting stable preinsertion state of remdesivir appeared to form hydrogen bonds with the RNA template when aligned with the newly solved cryo-EM structure of SARS-CoV-2 RdRp. | remdesivir | ORF1a polyprotein;ORF1ab polyprotein | Severe acute respiratory syndrome coronavirus 2 |
6 | The relative binding free energy between remdesivir and ATP was calculated to be -2.80 +- 0.84 kcal/mol, where remdesivir bound much stronger to SARS-CoV-2 RdRp than the natural substrate ATP. | remdesivir | ORF1a polyprotein;ORF1ab polyprotein | Severe acute respiratory syndrome coronavirus 2 |
7 | The relative binding free energy between remdesivir and ATP was calculated to be -2.80 +- 0.84 kcal/mol, where remdesivir bound much stronger to SARS-CoV-2 RdRp than the natural substrate ATP. | Adenosine Triphosphate | ORF1a polyprotein;ORF1ab polyprotein | Severe acute respiratory syndrome coronavirus 2 |
8 | The relative binding free energy between remdesivir and ATP was calculated to be -2.80 +- 0.84 kcal/mol, where remdesivir bound much stronger to SARS-CoV-2 RdRp than the natural substrate ATP. | remdesivir | ORF1a polyprotein;ORF1ab polyprotein | Severe acute respiratory syndrome coronavirus 2 |
9 | The ~100-fold improvement in the Kd from remdesivir over ATP indicates an effective replacement of ATP in blocking of the RdRp preinsertion site. | remdesivir | ORF1a polyprotein;ORF1ab polyprotein | Severe acute respiratory syndrome coronavirus 2 |
10 | The ~100-fold improvement in the Kd from remdesivir over ATP indicates an effective replacement of ATP in blocking of the RdRp preinsertion site. | Adenosine Triphosphate | ORF1a polyprotein;ORF1ab polyprotein | Severe acute respiratory syndrome coronavirus 2 |
11 | The ~100-fold improvement in the Kd from remdesivir over ATP indicates an effective replacement of ATP in blocking of the RdRp preinsertion site. | Adenosine Triphosphate | ORF1a polyprotein;ORF1ab polyprotein | Severe acute respiratory syndrome coronavirus 2 |