User:Jaime.Prilusky/Test/Sortable

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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by Eric Martz
A historical review on sculptures and physical models of macromolecules.

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ST Huber, D Terwiel, WH Evers, D Maresca, AJ Jakobi. Preprint 2022 doi: 10.1101/2022.05.08.489936
Many kinds of bacteria and archaea control their buoyancy to move to optimal positions in liquid environments. They do this by making nano-compartments called "gas vesicles", long "pipes" with closed ends filled with gases. In 2022, gas vesicle structure was solved, revealing self-assembling thin-walled cylinders of remarkable strength with gas-permeable pores and water-repelling (hydrophobic) interiors. Building on this structural knowledge, gas vesicles are being engineered to serve as biosensors that report via ultrasound.

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Above is a transmembrane protein that takes up, into your intestinal cells, orally consumed peptide nutrients and drugs. Its lumen-face (shown above) opens and binds peptide or drug, then closes, while its cytoplasmic face (opposite end from the above) opens to release its cargo into the intestinal cell, which passes it on into the blood circulation.

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