Nature Search

Cryo-EM structures of prokaryotic ligand-gated ion channel GLIC provide insights into gating in a lipid environment

Gloeobacter proton-gated ion channel (GLIC) is a convenient model of pentameric ligand-gated ion channels. Here, Bharambe & Li et al. report structures and simulations of GLIC with insights into the role of lipids in GLIC gating mechanism.

Nikhil Bharambe
Zhuowen Li
Sandip Basak
ResearchOpen Access05 Apr 2024
Nature Communications

Volume: 15, P: 1-16
Ecological restoration at pilot-scale employing site-specific rationales for small-patch degraded mangroves in Indian Sundarbans

Krishna Ray
Sandip Kumar Basak
Rahul Joshi
ResearchOpen Access05 Jun 2024
Scientific Reports

Volume: 14, P: 1-23
Molecular mechanism of setron-mediated inhibition of full-length 5-HT_3A receptor

Serotonin receptors (5-HT₃R) belong to the pentameric ligand-gated ion channel superfamily and mediate excitatory postsynaptic signaling. Here the authors present the high-resolution cryo-EM structure of 5-HT_3AR bound with the competitive antagonist granisetron and further validate the granisetron-binding mode with electrophysiology measurements and MD simulations.

Sandip Basak
Yvonne Gicheru
Sudha Chakrapani
ResearchOpen Access19 Jul 2019
Nature Communications

Volume: 10, P: 1-11
Mechanisms of activation and desensitization of full-length glycine receptor in lipid nanodiscs

Glycinergic synapses play a central role in motor control and pain processing in the central nervous system. Here, authors present cryo-EM structures of the full-length glycine receptors (GlyRs) reconstituted into lipid nanodiscs in the unliganded, glycine-bound and allosteric modulator-bound conformations and reveal global conformational changes underlying GlyR channel gating and modulation.

Arvind Kumar
Sandip Basak
Sudha Chakrapani
ResearchOpen Access27 Jul 2020
Nature Communications

Volume: 11, P: 1-14
Structural basis for cannabinoid-induced potentiation of alpha1-glycine receptors in lipid nanodiscs

Glycine receptors (GlyRs) mediate motor control and pain perception. Here, Kumar et al. present structures of GlyR bound to Δ9 -tetrahydrocannabinol (THC) using cryo-electron microscopy, providing insight into the therapeutic effects of cannabinoids.

Arvind Kumar
Kayla Kindig
Sudha Chakrapani
ResearchOpen Access18 Aug 2022
Nature Communications

Volume: 13, P: 1-14
Cryo-EM structure of 5-HT_3A receptor in its resting conformation

Serotonin receptor (5-HT_3AR), a pentameric ligand-gated ion channel, regulates numerous gastrointestinal functions. Here the authors provide a cryo-electron microscopic structure from the full-length 5-HT_3AR in the apo-state which corresponds to a resting conformation of the channel.

Sandip Basak
Yvonne Gicheru
Sudha Chakrapani
ResearchOpen Access06 Feb 2018
Nature Communications

Volume: 9, P: 1-10
Structural basis of TRPV5 channel inhibition by econazole revealed by cryo-EM

The cryo-EM structure of the full-length TRPV5 channel in complex with inhibitor econazole reveals a domain-swapped architecture and provides insights into mechanisms of inhibition.

Taylor E. T. Hughes
David T. Lodowski
Vera Y. Moiseenkova-Bell
Research01 Jan 2018
Nature Structural & Molecular Biology

Volume: 25, P: 53-60
Cryo-EM reveals two distinct serotonin-bound conformations of full-length 5-HT_3A receptor

Cryo-electron microscopy structures of the serotonin-bound 5-HT_3A serotonin receptor show the receptor populating two distinct states, characterized by twisting in the extracellular and transmembrane domains relative to the apo state, which creates pathways for ion permeation.

Sandip Basak
Yvonne Gicheru
Sudha Chakrapani
Research31 Oct 2018
Nature

Volume: 563, P: 270-274
Forecasting mangrove ecosystem degradation utilizing quantifiable eco-physiological resilience -A study from Indian Sundarbans

Mst Momtaj Begam
Rajojit Chowdhury
Krishna Ray
ResearchOpen Access21 Apr 2020
Scientific Reports

Volume: 10, P: 1-14

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