Molecular Structure of the Human CFTR Ion Channel
نویسندگان
چکیده
منابع مشابه
Molecular Structure of the Human CFTR Ion Channel
The cystic fibrosis transmembrane conductance regulator (CFTR) is an ATP-binding cassette (ABC) transporter that uniquely functions as an ion channel. Here, we present a 3.9 Å structure of dephosphorylated human CFTR without nucleotides, determined by electron cryomicroscopy (cryo-EM). Close resemblance of this human CFTR structure to zebrafish CFTR under identical conditions reinforces its rel...
متن کاملIdentification of an ion channel-forming motif in the primary structure of CFTR, the cystic fibrosis chloride channel.
Synthetic peptides with sequences representing putative transmembrane (M) segments of CFTR (the cystic fibrosis transmembrane conductance regulator) were used as tools to identify the involvement of such segments in forming the ionic pore of the CFTR Cl- channel. Peptides with sequences corresponding to M2 and M6 form anion-selective channels after reconstitution in lipid bilayers. In contrast,...
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15 صفحه اولThe CFTR ion channel: gating, regulation, and anion permeation.
Cystic fibrosis transmembrane conductance regulator (CFTR) is an ATP-gated anion channel with two remarkable distinctions. First, it is the only ATP-binding cassette (ABC) transporter that is known to be an ion channel--almost all others function as transport ATPases. Second, CFTR is the only ligand-gated channel that consumes its ligand (ATP) during the gating cycle--a consequence of its enzym...
متن کاملStructure and function of the CFTR chloride channel.
Structure and Function of the CFTR Chloride Channel. Physiol. Rev. 79, Suppl.: S23-S45, 1999. - The cystic fibrosis transmembrane conductance regulator (CFTR) is a unique member of the ABC transporter family that forms a novel Cl- channel. It is located predominantly in the apical membrane of epithelia where it mediates transepithelial salt and liquid movement. Dysfunction of CFTR causes the ge...
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ژورنال
عنوان ژورنال: Cell
سال: 2017
ISSN: 0092-8674
DOI: 10.1016/j.cell.2017.02.024