Magnesium site in human oncochannel TRPV6 is formed by two negatively charged residues that are close together in the closed state and separated in the open state. Mg2+ binding keeps these residues together and stabilizes the closed state. With Chubanov/Efremov labs! www.nature.com/articles/s41...

Magnesium site in TRPV6 is formed by two negatively charged residues that are close together in the closed state and separated in the open. Magnesium binding keeps them together and stabilizes the closed state. Amazing collaboration with Chubanov and Efremov groups. www.nature.com/articles/s41...

Magnesium site in TRPV6 is formed by two negatively charged residues that are close together in the closed state and separated in the open. Magnesium binding keeps them together and stabilizes the closed state. Amazing collaboration with Chubanov and Efremov groups.
www.nature.com/articles/s41...

Happy to share the locking mechanism of human oncochannel TRPV6 inhibition by intracellular magnesium. Amazing collaboration with Chubanov and Efremov groups. www.nature.com/articles/s41...

Happy to share our new review of kainate receptor structure and gating. www.frontiersin.org/journals/pha...

Happy to share the molecular mechanism of activation of kainate-subtype ionotropic glutamate receptor GluK2 in complex with auxiliary subunits Neto2. In both closed/apo and open states, ligand-binding domain (LBD) layer has 2-fold rotational symmetry!
www.nature.com/articles/s41...