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by Eric Martz
Coronavirus SARS-CoV-2 (responsible for COVID-19) has a spike protein on its surface, which enables it to infect host cells. Initially, proteases in the lungs clip the homo-trimeric spike protein at a unique sequence. This primes it, causing it to extend its receptor binding surface (shown in the above animation), optimizing binding to the host cell's ACE2 receptor (not shown). Next, spike protein initiates fusion of the virus and host cell membranes (not shown), enabling the virus RNA to enter the cell and initiate production of new virions. Knowledge of spike protein's molecular structure and function is crucial to developing effective therapies and vaccines.
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G Atilla-Gocumen, L Di Costanzo, E Meggers. J Biol Inorg Chem. 2010 doi: 10.1007/s00775-010-0699-x
A crystal structure of an organometallic half-sandwich ruthenium complex bound to glycogen synthase kinase 3ß (GSK-3ß) reveals that the inhibitor binds to the ATP binding site via an induced fit mechanism utilizing several hydrogen bonds and hydrophobic interactions. Importantly, the metal is not involved in any direct interaction with the protein kinase but fulfills a purely structural role.

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Touching stretches cell membranes, opening mechanosensitive ion channels, leading to sensation by the nervous system. Pictured is the transmembrane region of a similar channel in bacteria. When closed, the narrow opening is lined by hydrophobic amino acid sidechains, making it non-conductive to ions.

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