Journal:Acta Cryst D:S2059798322007677
From Proteopedia
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<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| + | SARS-CoV-2 initiates infection of host cells by anchoring its viral envelope spike protein to the ACE2 receptor on the surface of human cells. Since its initial identification, a remarkable number of variants and other yet unmonitored lineages have been detected. Most of them harbor amino acid mutations in the spike protein with the potential to modulate the strength of the spike:ACE2 interaction. Further, some mutations can ultimately lead to immune evasion and reduction of the efficacy of existing vaccines. | ||
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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; doi: 10.1038/s41467-022-28246-3]. | ||
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| + | 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. | ||
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 10:06, 1 August 2022
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