SARS-CoV-2 spike protein fusion transformation: Difference between revisions
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===More Compact Structure=== | ===More Compact Structure=== | ||
Previous studies of soluble extracellular portions of the spike protein have utilized a double proline mutation (K986P, V987P) that stabilizes the pre-fusion conformation<ref name="cai-zhang" /><ref name="wrobel">PMID:32647346</ref>. K986P appears to eliminate a salt bridge, causing an unsatisfied internal charge<ref name="cai-zhang" />. The wild type salt bridge may contribute to the more compact and better resolved structure observed by Cai, Zhang and coworkers<ref name="cai-zhang" /> using the full-length wild type protein. | Previous studies of soluble extracellular portions of the spike protein have utilized a double proline mutation (K986P, V987P) that stabilizes the pre-fusion conformation<ref name="cai-zhang" /><ref name="wrobel">PMID:32647346</ref>. K986P appears to eliminate a salt bridge, causing an unsatisfied internal charge<ref name="cai-zhang" />. The wild type salt bridge may contribute to the more compact and better resolved structure observed by Cai, Zhang and coworkers<ref name="cai-zhang" /> using the full-length wild type protein. | ||
==Preventing Fusion with Drugs=== | |||
SARS-CoV-2 spike protein has two interior cavities. The larger interior cavity opens to the surface when [[SARS-CoV-2_protein_S_priming_by_furin|one receptor binding site is extended]]. The smaller interior cavity is required for the fusion transformation. Using virtual screening simulations, Romeo, Iacovelli & Falconi<ref name="romeo">PMID: 32565126</ref> identified available drugs that seem likely to block the fusion transformation by binding in the smaller cavity. | |||