Asset Details
Do you wish to reserve the book?
The Cryo-EM structure of pannexin 1 reveals unique motifs for ion selection and inhibition
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
The Cryo-EM structure of pannexin 1 reveals unique motifs for ion selection and inhibition
Do you wish to request the book?
The Cryo-EM structure of pannexin 1 reveals unique motifs for ion selection and inhibition
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
The Cryo-EM structure of pannexin 1 reveals unique motifs for ion selection and inhibition
2020
Overview
Pannexins are large-pore forming channels responsible for ATP release under a variety of physiological and pathological conditions. Although predicted to share similar membrane topology with other large-pore forming proteins such as connexins, innexins, and LRRC8, pannexins have minimal sequence similarity to these protein families. Here, we present the cryo-EM structure of a frog pannexin 1 (Panx1) channel at 3.0 Å. We find that Panx1 protomers harbor four transmembrane helices similar in arrangement to other large-pore forming proteins but assemble as a heptameric channel with a unique constriction formed by Trp74 in the first extracellular loop. Mutating Trp74 or the nearby Arg75 disrupt ion selectivity, whereas altering residues in the hydrophobic groove formed by the two extracellular loops abrogates channel inhibition by carbenoxolone. Our structural and functional study establishes the extracellular loops as important structural motifs for ion selectivity and channel inhibition in Panx1.
Publisher
eLife Science Publications, Ltd,eLife Sciences Publications Ltd,eLife Sciences Publications, Ltd
Subject
/ Animals
/ Carbenoxolone - pharmacology
/ Connexins - antagonists & inhibitors
/ EDTA
/ Humans
/ Kinases
/ pannexin
/ Proteins
/ Structural Biology and Molecular Biophysics
/ Structure-function relationships
/ Xenopus Proteins - antagonists & inhibitors
/ Xenopus Proteins - chemistry
