Cryo-electron microscopy data of thermostabilized avian CFTR
Ontology highlight
ABSTRACT:
SUBMITTER: Jonathan Firoze fay
PROVIDER: EMPIAR-10219 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Cryo-EM Visualization of an Active High Open Probability CFTR Anion Channel.
Fay Jonathan F JF Aleksandrov Luba A LA Jensen Timothy J TJ Cui Liying L LL Kousouros Joseph N JN He Lihua L Aleksandrov Andrei A AA Gingerich Drew S DS Riordan John R JR Chen James Z JZ
Biochemistry 20181016 43
The cystic fibrosis transmembrane conductance regulator (CFTR) anion channel, crucial to epithelial salt and water homeostasis, and defective due to mutations in its gene in patients with cystic fibrosis, is a unique member of the large family of ATP-binding cassette transport proteins. Regulation of CFTR channel activity is stringently controlled by phosphorylation and nucleotide binding. Structural changes that underlie transitions between active and inactive functional states are not yet full ...[more]
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