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Giant single-crystal-to-single-crystal transformations associated with chiral interconversion induced by elimination of chelating ligands

Crystalline materials that undergo large structural changes in response to external stimuli remain rare. Here the authors report a Zinc(II) complex that undergoes a two-step reversible single-crystal-to-single-crystal transformation via thermal removal of ethylene glycol chelating ligands; this results in large volume changes.

Yun Li
Bo Zhao
Jun Tao
ResearchOpen Access25 Nov 2021
Nature Communications

Volume: 12, P: 1-8
Ligand recognition and G protein coupling of the human itch receptor MRGPRX1

MRGPRX1 is a key GPCR expressed in the DRG for itch perception, generating scratch or avoidance behaviors. Here, authors provide structural and pharmacological insights into itch sensation, activation and G-protein signaling downstream of MRGPRX1.

Lulu Guo
Yumu Zhang
Jin-Peng Sun
ResearchOpen Access17 Aug 2023
Nature Communications

Volume: 14, P: 1-12
Structural insights into the mechanisms of urea permeation and distinct inhibition modes of urea transporters

Here, authors present cryo-EM structures and simulations of urea transporter members in resting-, transport-, or inactive-states bound with synthetic competitive, uncompetitive or noncompetitive inhibitor.

Shen-Ming Huang
Zhi-Zhen Huang
Jin-Peng Sun
ResearchOpen Access26 Nov 2024
Nature Communications

Volume: 15, P: 1-17
Functional screening and rational design of compounds targeting GPR132 to treat diabetes

This study presents a comprehensive pipeline to profile transmembrane receptors involved in macrophage-driven inflammation in pancreatic islets during the onset of diabetes. The authors identify GPR132 as a mediator of macrophage-driven inflammation and find compounds that reduce inflammation and improve glycaemic control.

Jia-Le Wang
Xiao-Dong Dou
Xiao Yu
Research28 Sept 2023
Nature Metabolism

Volume: 5, P: 1726-1746
Structures of the ADGRG2–G_s complex in apo and ligand-bound forms

The description of the cryo-EM structure of an orphan adhesion GPCR–G_s protein complex in apo state facilitates the screening and identification of potential ligands of ADGRG2.

Hui Lin
Peng Xiao
Xiao Yu
Research18 Aug 2022
Nature Chemical Biology

Volume: 18, P: 1196-1203
Spontaneous rotational symmetry breaking in KTaO₃ heterointerface superconductors

Superconducting interfaces involving KTaO3 have recently attracted attention due to their relatively high transition temperature. Here, the authors study amorphous-YAlO₃/KTaO₃ interfaces and find two-fold symmetry in the superconducting regime, possibly due to a mixed-parity superconducting state.

Guanqun Zhang
Lijie Wang
Wei Li
ResearchOpen Access26 May 2023
Nature Communications

Volume: 14, P: 1-8
A spin-crossover framework endowed with pore-adjustable behavior by slow structural dynamics

Host-guest interactions can play a critical role in achieving switchable porous materials, but controlling them remains challenging. Here the authors report an atypical pore rearrangement in a magnetic 2D porous framework upon water adsorption; the structural transformation affects the magnetic properties of the material.

Jin-Peng Xue
Yang Hu
Jun Tao
ResearchOpen Access18 Jun 2022
Nature Communications

Volume: 13, P: 1-10
Arrestin-biased AT1R agonism induces acute catecholamine secretion through TRPC3 coupling

Angiotensin II type 1 receptor (AT1R)-mediated acute catecholamine release is modulated by β-arrestin. Here the authors show that β-arrestin-1 recruits the Ca²⁺channel TRPC3 and the PLCγ to the AT1R-β-arrestin complex, triggering G protein-independent calcium influx and catecholamine secretion.

Chun-Hua Liu
Zheng Gong
Jin-Peng Sun
ResearchOpen Access09 Feb 2017
Nature Communications

Volume: 8, P: 1-17
Structural characterization of the urea transporter bound to the orally bioavailable inhibitor E3

Shen-ming Huang
Bo-yang Cai
Jin-peng Sun
Research16 Jun 2025
Acta Pharmacologica Sinica

P: 1-9
DeSiphering receptor core-induced and ligand-dependent conformational changes in arrestin via genetic encoded trimethylsilyl ¹H-NMR probe

Characterization of dynamic conformational changes in membrane protein complexes by NMR spectroscopy remains challenging. Here authors report the site-specific incorporation of 4-trimethylsilyl phenylalanine (TMSiPhe) into proteins, which enabled the characterization of multiple conformational states of a phospho-β2 adrenergic receptor/β-arrestin-1 complex in response to different receptor ligands.

Qi Liu
Qing-tao He
Jin-peng Sun
ResearchOpen Access25 Sept 2020
Nature Communications

Volume: 11, P: 1-17
Phospho-selective mechanisms of arrestin conformations and functions revealed by unnatural amino acid incorporation and ¹⁹F-NMR

G-protein-coupled receptors (GPCRs) signal via G proteins or arrestin-mediated pathways; the plasticity of arrestin proteins is thought to underlie their function. Here, the authors use NMR to examine how β-arrestin-1 recognizes different GPCR phospho-barcodes, and how this triggers structural rearrangements to fulfill selective functions.

Fan Yang
Xiao Yu
Jin-Peng Sun
ResearchOpen Access08 Sept 2015
Nature Communications

Volume: 6, P: 1-15
In vitro expansion of pancreatic islet clusters facilitated by hormones and chemicals

Jing-Yu Lin
Jie Cheng
Xiao Yu
ResearchOpen Access07 Apr 2020
Cell Discovery

Volume: 6, P: 1-12

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