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	Structures of human pannexin 1 reveal ion pathways and mechanism of gating.
Journal, issue, pages	Nature, Vol. 584, Issue 7822, Page 646-651, Year 2020
Publish date	Jun 3, 2020
Authors	Zheng Ruan / Ian J Orozco / Juan Du / Wei Lü /
PubMed Abstract	Pannexin 1 (PANX1) is an ATP-permeable channel with critical roles in a variety of physiological functions such as blood pressure regulation, apoptotic cell clearance and human oocyte development. ...Pannexin 1 (PANX1) is an ATP-permeable channel with critical roles in a variety of physiological functions such as blood pressure regulation, apoptotic cell clearance and human oocyte development. Here we present several structures of human PANX1 in a heptameric assembly at resolutions of up to 2.8 angström, including an apo state, a caspase-7-cleaved state and a carbenoxolone-bound state. We reveal a gating mechanism that involves two ion-conducting pathways. Under normal cellular conditions, the intracellular entry of the wide main pore is physically plugged by the C-terminal tail. Small anions are conducted through narrow tunnels in the intracellular domain. These tunnels connect to the main pore and are gated by a long linker between the N-terminal helix and the first transmembrane helix. During apoptosis, the C-terminal tail is cleaved by caspase, allowing the release of ATP through the main pore. We identified a carbenoxolone-binding site embraced by W74 in the extracellular entrance and a role for carbenoxolone as a channel blocker. We identified a gap-junction-like structure using a glycosylation-deficient mutant, N255A. Our studies provide a solid foundation for understanding the molecular mechanisms underlying the channel gating and inhibition of PANX1 and related large-pore channels.
External links	Nature / PubMed:32494015 / PubMed Central
Methods	EM (single particle)
Resolution	2.83 - 6.04 Å
Structure data	21588 6wbf EMDB-21588, PDB-6wbf: Cryo-EM structure of wild type human Pannexin 1 channel Method: EM (single particle) / Resolution: 2.83 Å 21589 6wbg EMDB-21589, PDB-6wbg: Cryo-EM structure of human Pannexin 1 channel with its C-terminal tail cleaved by caspase-7 Method: EM (single particle) / Resolution: 2.97 Å 21590 6wbi EMDB-21590, PDB-6wbi: Cryo-EM structure of human Pannexin 1 channel with its C-terminal tail cleaved by caspase-7, in complex with CBX Method: EM (single particle) / Resolution: 4.39 Å 21591 6wbk EMDB-21591, PDB-6wbk: Cryo-EM structure of human Pannexin 1 channel with deletion of N-terminal helix and C-terminal tail Method: EM (single particle) / Resolution: 6.01 Å 21592 6wbl EMDB-21592, PDB-6wbl: Cryo-EM structure of human Pannexin 1 channel with deletion of N-terminal helix and C-terminal tail, in complex with CBX Method: EM (single particle) / Resolution: 5.13 Å 21593 6wbm EMDB-21593, PDB-6wbm: Cryo-EM structure of human Pannexin 1 channel N255A mutant Method: EM (single particle) / Resolution: 2.86 Å 21594 6wbn EMDB-21594, PDB-6wbn: Cryo-EM structure of human Pannexin 1 channel N255A mutant, gap junction Method: EM (single particle) / Resolution: 2.83 Å EMDB-21595: Cryo-EM structure of wild type human Pannexin 1 channel in the presence of EDTA Method: EM (single particle) / Resolution: 3.01 Å EMDB-21596: Cryo-EM structure of wild type human Pannexin 1 channel in the presence of 5 mM calcium Method: EM (single particle) / Resolution: 3.04 Å EMDB-21597: Cryo-EM structure of wild type human Pannexin 1 channel in the presence of 150 mM KCl Method: EM (single particle) / Resolution: 3.15 Å EMDB-21598: Cryo-EM structure of wild type human Pannexin 1 channel extracted using SMA 30010 Method: EM (single particle) / Resolution: 6.04 Å
Chemicals	ChemComp-PTY: PHOSPHATIDYLETHANOLAMINE / phospholipidYM ChemComp-3PE: 1,2-Distearoyl-sn-glycerophosphoethanolamine / phospholipidYM ChemComp-DGA: DIACYL GLYCEROL ChemComp-CLR: CHOLESTEROL ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose ChemComp-CBO: CARBENOXOLONE
Source	homo sapiens (human)
Keywords	TRANSPORT PROTEIN / ion channel