Sign in

Hideaki E. Kato

@emekato.bsky.social
231 followers 62 following 13 posts

Professor at UTokyo. (postdoc @Stanford) / b.1986 / structural biology, protein engineering, rhodopsin, GPCRs tinyurl.com/ycyf87t7

PostsRepliesMedia
Hideaki E. Kato @emekato.bsky.social · 08/04/2026
We present NOAH-ARK: combining de novo marker design ARK1 with in silico linker optimization program NOAH enables semi-automated, high-resolution GPCR structures—clear enough to resolve ligands, waters, and ions. (2/2)
051
Hideaki E. Kato @emekato.bsky.social · 08/04/2026
www.biorxiv.org/content/10.6... New preprint from our lab! Solving antagonist-bound GPCR structures is becoming easier with fusion markers, but linker optimization between GPCR and marker is still a bottleneck. (1/2)
142
Hideaki E. Kato @emekato.bsky.social · 08/04/2026
A little late, but we had a chance to have a small celebration in the lab today. (We actually had a celebration dinner several weeks ago, but I forgot to take photos at that time...) Again, congrats to everyone involved!
020
Hideaki E. Kato @emekato.bsky.social · 14/03/2026
Thanks Daniel!
000
Hideaki E. Kato @emekato.bsky.social · 11/03/2026
Happy to share our work on conventional and time-resolved cryo-EM studies of NTSR1, now published in Nature! nature.com/articles/s41... Wonderful collab. w/ Sumino, Mitsutake, Kobilka, & Inoue labs. Congrats to Kazuhiro, Kouki, Toshiki, Shun & everyone involved!
nature.com
The dynamic basis of G-protein recognition and activation by a GPCR - Nature
Conventional and time-resolved cryo-electron microscopy reveal how NTSR1 dynamically engages and releases different G proteins, capturing over 20 intermediates and uncovering key mechanistic step...
2155
Hideaki E. Kato @emekato.bsky.social · 18/09/2025
Happy to share our new preprint on the red-shifted channelrhodopsin ChR024, recently discovered by Inoue Lab (biorxiv.org/content/10.1... ), highlighting its long-wavelength absorption and ion conductance: biorxiv.org/content/10.1... Many thanks to our wonderful lab members and collaborators!
095
Hideaki E. Kato @emekato.bsky.social · 26/03/2025
000
Hideaki E. Kato @emekato.bsky.social · 26/03/2025
(3) Contrary to prior assumptions, 4‑CMTB, an FFA2‑specific ago‑PAM, binds the outer surface of TM6‑7, stabilizing it and shifting FFA2 equilibrium to its active state. Notably, although this pocket is unique to active FFA2, one mutation permits the activation of FFA3 by 4‑CMTB.
100
Hideaki E. Kato @emekato.bsky.social · 26/03/2025
(2) The binding site of FFA2 antagonist, GLPG0974 has been controversial. Our data show that this compd binds just next to the ortho pocket, pushing the Tyr residue that separates the ortho and allosteric pockets and clashing with the ortho pocket; this Tyr residue acts as a micro‑lever switch.
100
Hideaki E. Kato @emekato.bsky.social · 26/03/2025
(1) Wild‑type FFA2 is normally activated only by short‑chain fatty acids; however, when the ligand entry site is tuned, it can also be activated by long‑chain fatty acids!
100
Hideaki E. Kato @emekato.bsky.social · 26/03/2025
We solved the cryo‑EM structures of (I) the active FFA2‑Gi complex with TUG‑1375 and 4‑CMTB, and (II) the inactive FFA2 in complex with GLPG0974. In combination with simulations and cell-based assays, we found several interesting things…, I’d like to highlight three key findings in this paper:
100
Hideaki E. Kato @emekato.bsky.social · 26/03/2025
Happy to share our work on the ligand selectivity and allosteric regulation of FFA2 using a combination of cryo‑EM, MD simulations, and mol. pharmacology! It was a great collab. with Ishikita, Dror, and Inoue labs. Congrats to Mai, Kouki, Ryoji, and everyone involved! www.nature.com/articles/s41...
180
Hideaki E. Kato @emekato.bsky.social · 23/11/2024
Just made my account in BlueSky...
091