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...

Pleasure to be part of this work www.pnas.org/doi/10.1073/... with Sandip Basak at NTU where we show asymmetric gating in GLIC!

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

Congratulations, Yifan, for the Anatrace Award! Yifan’s work on the TRPV1 structure with David Julius helped launch the Resolution Revolution in cryo-EM. Not just in membrane proteins—hardly any area of biophysics today has remained untouched by the techniques Yifan pioneered.

Cryo-EM snapshots of NMDA receptor activation illuminate sequential rearrangements | Science Advances www.science.org/doi/10.1126/...

How the twin-arginine translocase (Tat) system manages to transport folded proteins across membranes without any leaks? To answer this fundamental question we solved the first structure of TatB3C3 complex with bound cargo. Please check out new preprint! t.co/962Kj9pt6F

🚨🧠🔬 A major breakthrough in molecular neuroscience: I am excited to share a new story from our lab, published in accelerated format today by @nature.com: "Delta-type glutamate receptors are ligand-gated ion channels" Read more here (free article link): rdcu.be/eGIKz

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...

Happy to share our new review on the structural pharmacology of TRP channels! Check out the supplementary table, which includes a list of all ligands, corresponding PDBs of complexes with TRP channels, and reported affinity values. www.sciencedirect.com/science/arti... #ionchannel #TRPchannel (1/5)