Journal:Acta Cryst D:S2059798322007677
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In this work, we study the molecular bases that underlie the enhanced adherence to ACE2 conferred by the mutation Q498Y, located in the SARS-CoV-2 spike receptor binding domain (RBD). This substitution has been found in SARS-CoV-2 human samples and others of unknown origin [GISAID DATABASE <ref>doi: 10.1038/s41467-022-28246-3</ref>]. | In this work, we study the molecular bases that underlie the enhanced adherence to ACE2 conferred by the mutation Q498Y, located in the SARS-CoV-2 spike receptor binding domain (RBD). This substitution has been found in SARS-CoV-2 human samples and others of unknown origin [GISAID DATABASE <ref>doi: 10.1038/s41467-022-28246-3</ref>]. | ||
| - | <scene name='91/918482/Cv/2'>Composition of the asymmetric unit in the RBD Q498Y:ACE2 crystal</scene>. All RBD and ACE2 molecules are shown in individual colored cartoons. < | + | <scene name='91/918482/Cv/2'>Composition of the asymmetric unit in the RBD Q498Y:ACE2 crystal</scene>. All RBD and ACE2 molecules are shown in individual colored cartoons. |
| + | *<scene name='91/918482/Cv/3'>Asymmetric unit copy 1</scene>. | ||
| + | *<scene name='91/918482/Cv/4'>Asymmetric unit copy 2</scene>. | ||
| + | *<scene name='91/918482/Cv/2'>Both copies of asymmetric unit</scene>. | ||
| - | Our studies conclude that the increased affinity of the Q498Y RBD protein is due to a higher number and types of inter-molecular interactions provided by the RBD tyrosine 498 side chain, compared to those associated to glutamine 498 in the wild-type RBD. | + | Our studies conclude that the increased affinity of the Q498Y RBD protein is due to a higher number and types of inter-molecular interactions provided by the RBD tyrosine 498 side chain, compared to those associated to glutamine 498 in the wild-type RBD. Comparison of the interatomic contacts between RBD and ACE2 in the wild type and Q498Y structures: |
| + | *<scene name='91/918482/Cv/10'>Interatomic polar interactions</scene> are shown as white dashed lines. The cut-off for Van der Waals and H-bonds are set to 4 Å and 3.4 Å, respectively. Interacting residues are depicted as sticks. | ||
| + | <jmol><jmolButton><script>frame 2 2 play; animation off; frame 2</script><text>only wild type structure</text></jmolButton><jmolButton><script>frame 1 1 play; animation off; frame 1</script><text>only Q498Y structure</text></jmolButton><jmolButton><script>animation off; frame all</script><text>both wild type and Q498Y</text></jmolButton></jmol> | ||
| + | *<scene name='91/918482/Cv1/2'>Interatomic non-polar interactions</scene> are indicated as dashed lines. | ||
| + | <jmol><jmolButton><script>frame 2 2 play; animation off; frame 2</script><text>only wild type structure</text></jmolButton><jmolButton><script>frame 1 1 play; animation off; frame 1</script><text>only Q498Y structure</text></jmolButton><jmolButton><script>animation off; frame all</script><text>both wild type and Q498Y</text></jmolButton></jmol> | ||
| + | *<scene name='91/918482/Cv1/3'>π-π stacking interaction established between the RBD Tyr498 and ACE2 Tyr41 aromatic rings</scene> | ||
| + | <jmol><jmolButton><script>frame 2 2 play; animation off; frame 2</script><text>only wild type structure</text></jmolButton><jmolButton><script>frame 1 1 play; animation off; frame 1</script><text>only Q498Y structure</text></jmolButton><jmolButton><script>animation off; frame all</script><text>both wild type and Q498Y</text></jmolButton></jmol> | ||
<b>References</b><br> | <b>References</b><br> | ||
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