@sobolevsky.bsky.social
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...
November 6, 2025 at 6:07 PM
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...
November 6, 2025 at 5:49 PM
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...
www.nature.com/articles/s41...
November 6, 2025 at 5:48 PM
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...
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...
November 6, 2025 at 5:45 PM
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...
Reposted
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!
Asymmetric gating of a homopentameric ion channel GLIC revealed by cryo-EM | PNAS
Pentameric ligand-gated ion channels (pLGICs) are vital neurotransmitter receptors
that are key therapeutic targets for neurological disorders. Alt...
www.pnas.org
October 23, 2025 at 4:24 PM
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...
October 20, 2025 at 7:14 PM
Happy to share our new review of kainate receptor structure and gating. www.frontiersin.org/journals/pha...
Reposted
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.
Yifan Cheng to Receive 2026 Anatrace Membrane Protein Award buff.ly/ooI1UDy
September 24, 2025 at 10:09 PM
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.
Reposted
Cryo-EM snapshots of NMDA receptor activation illuminate sequential rearrangements | Science Advances www.science.org/doi/10.1126/...
Cryo-EM snapshots of NMDA receptor activation illuminate sequential rearrangements
Opening of the NMDA receptor involves bending of the helices lining the ion channel gate.
www.science.org
September 24, 2025 at 6:39 PM
Cryo-EM snapshots of NMDA receptor activation illuminate sequential rearrangements | Science Advances www.science.org/doi/10.1126/...
Reposted
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
t.co/962Kj9pt6F
https://www.biorxiv.org/content/10.1101/2025.09.16.676506v1
t.co
September 18, 2025 at 5:35 PM
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
t.co/962Kj9pt6F
Reposted
🚨🧠🔬 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
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
September 16, 2025 at 4:47 PM
🚨🧠🔬 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
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...
www.nature.com/articles/s41...
September 11, 2025 at 1:17 PM
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...
www.nature.com/articles/s41...
Reposted
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)
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)
December 1, 2024 at 3:00 AM
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)
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)