Journal:Acta Cryst D:S2059798322007677
From Proteopedia
(Difference between revisions)
| Line 8: | Line 8: | ||
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. <jmol><jmolButton><script>display:A | + | <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. <jmol><jmolButton><script>display:A+E</script><text>only CtcP</text></jmolButton><jmolButton><script>display:B,C</script><text>only PltM</text></jmolButton><jmolButton><script>display all</script><text>both CtcP and PltM</text></jmolButton></jmol> |
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. | ||
Revision as of 12:39, 1 August 2022
| |||||||||||
This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
