Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural basis of PANX1 permeation and positive modulation by mefloquine.
Journal, issue, pages	Nat Commun, Vol. 16, Issue 1, Page 11057, Year 2025
Publish date	Dec 11, 2025
Authors	Yangyang Li / Zheng Ruan / Junuk Lee / Ian J Orozco / Edward Zhou / Juan Du / Wei Lü /
PubMed Abstract	Purinergic signaling relies on ATP release through exocytosis and large-pore channels. Large-pore channels permeate both small anions like chloride and large signaling molecules like ATP, but how ...Purinergic signaling relies on ATP release through exocytosis and large-pore channels. Large-pore channels permeate both small anions like chloride and large signaling molecules like ATP, but how this broad cargo selectivity is structurally controlled remains elusive. Here we investigate PANX1, a prototypical large-pore channel, and uncover structural plasticity at the extracellular entrance formed by seven tryptophan (W74) residues. The W74 sidechains are flexible, sampling conformations that range from a constricted state permissive only to chloride to a dilated state compatible with ATP. These states are coupled to variable cation-π interactions between W74 and arginine 75 (R75), suggesting a mechanism for dynamic tuning of pore architecture and selective cargo permeation. We also identify mefloquine as a positive modulator of PANX1 that binds near the side tunnel to control ion flow through this pathway. Together, these findings define the structural principles underlying PANX1 permeation and modulation.
External links	Nat Commun / PubMed:41381453 / PubMed Central
Methods	EM (single particle)
Resolution	2.5 - 3.45 Å
Structure data	70760 9oqg EMDB-70760, PDB-9oqg: Human pannexin 1 channel with 0 mM ATP Method: EM (single particle) / Resolution: 2.58 Å 70761 9oqh EMDB-70761, PDB-9oqh: Human pannexin 1 channel with 10 mM ATP Method: EM (single particle) / Resolution: 2.58 Å 70762 9oqi EMDB-70762, PDB-9oqi: Human pannexin 1 channel with 20 mM ATP Method: EM (single particle) / Resolution: 2.66 Å 70763 9oqj EMDB-70763, PDB-9oqj: Human pannexin 1 channel with 30 mM ATP Method: EM (single particle) / Resolution: 2.66 Å 70764 9oqk EMDB-70764, PDB-9oqk: Human pannexin 1 channel from combined 0, 10, 20, 30 mM ATP datasets Method: EM (single particle) / Resolution: 2.5 Å 70765 9oql EMDB-70765, PDB-9oql: Putative ATP-bound class from combined 10, 20, 30 mM ATP datasets Method: EM (single particle) / Resolution: 2.77 Å 70766 9oqm EMDB-70766, PDB-9oqm: Apo class from combined 0, 10, 20, 30 mM ATP datastes Method: EM (single particle) / Resolution: 2.8 Å 70767 9oqn EMDB-70767, PDB-9oqn: Constricted-pore class from combined 0, 10, 20, 30 mM ATP datasets Method: EM (single particle) / Resolution: 3.19 Å 70768 9oqo EMDB-70768, PDB-9oqo: Dilated-pore class from combined 0, 10, 20, 30 mM ATP datasets Method: EM (single particle) / Resolution: 3.45 Å 70769 9oqp EMDB-70769, PDB-9oqp: Human pannexin 1 channel with 1mM mefloquine Method: EM (single particle) / Resolution: 2.62 Å 70770 9oqq EMDB-70770, PDB-9oqq: Human pannexin 1 channel W74A mutant with 10mM ATP Method: EM (single particle) / Resolution: 3.25 Å
Chemicals	ChemComp-PTY: PHOSPHATIDYLETHANOLAMINE / phospholipidYM ChemComp-CLR: CHOLESTEROL ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM PDB-1a1v: HEPATITIS C VIRUS NS3 HELICASE DOMAIN COMPLEXED WITH SINGLE STRANDED SDNA
Source	homo sapiens (human) Human respiratory syncytial virus
Keywords	TRANSPORT PROTEIN / Pannexin 1 / ATP release / large-pore ion channel / membrane protein / Pannexin 1 channel with mefloquine / PANX1 / Pannexin / Large pore channel