- EMDB-28902: Cryo-EM structure of human pannexin 2 -
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Database: EMDB / ID: EMD-28902
Title
Cryo-EM structure of human pannexin 2
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Sample
Organelle or cellular component: human pannexin 2
Protein or peptide: Pannexin-2, Soluble cytochrome b562 fusion
Function / homology
Function and homology information
Electric Transmission Across Gap Junctions / wide pore channel activity / positive regulation of interleukin-1 production / monoatomic cation transport / monoatomic ion transmembrane transport / response to ischemia / electron transport chain / cell-cell signaling / periplasmic space / electron transfer activity ...Electric Transmission Across Gap Junctions / wide pore channel activity / positive regulation of interleukin-1 production / monoatomic cation transport / monoatomic ion transmembrane transport / response to ischemia / electron transport chain / cell-cell signaling / periplasmic space / electron transfer activity / iron ion binding / Golgi membrane / heme binding / endoplasmic reticulum membrane / structural molecule activity / plasma membrane Similarity search - Function
National Institutes of Health/National Institute of Neurological Disorders and Stroke (NIH/NINDS)
R01NS109307
United States
Citation
Journal: Nat Commun / Year: 2023 Title: Structural and functional analysis of human pannexin 2 channel. Authors: Zhihui He / Yonghui Zhao / Michael J Rau / James A J Fitzpatrick / Rajan Sah / Hongzhen Hu / Peng Yuan / Abstract: The pannexin 2 channel (PANX2) participates in multiple physiological processes including skin homeostasis, neuronal development, and ischemia-induced brain injury. However, the molecular basis of ...The pannexin 2 channel (PANX2) participates in multiple physiological processes including skin homeostasis, neuronal development, and ischemia-induced brain injury. However, the molecular basis of PANX2 channel function remains largely unknown. Here, we present a cryo-electron microscopy structure of human PANX2, which reveals pore properties contrasting with those of the intensely studied paralog PANX1. The extracellular selectivity filter, defined by a ring of basic residues, more closely resembles that of the distantly related volume-regulated anion channel (VRAC) LRRC8A, rather than PANX1. Furthermore, we show that PANX2 displays a similar anion permeability sequence as VRAC, and that PANX2 channel activity is inhibited by a commonly used VRAC inhibitor, DCPIB. Thus, the shared channel properties between PANX2 and VRAC may complicate dissection of their cellular functions through pharmacological manipulation. Collectively, our structural and functional analysis provides a framework for development of PANX2-specific reagents that are needed for better understanding of channel physiology and pathophysiology.
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